http://journals.iucr.org/f/issues/2013/06/00/isscontsbdy.html Acta Crystallographica Section F: Structural Biology and Crystallization Communications is a rapid all-electronic journal, which provides a home for short communications on the crystallization and structure of biological macromolecules. Structures determined through structural genomics initiatives or from iterative studies such as those used in the pharmaceutical industry are particularly welcomed. Articles are available online when ready, making publication as fast as possible, and include unlimited free colour illustrations, movies and other enhancements. The editorial process is completely electronic with respect to deposition, submission, refereeing and publication. en Copyright (c) 2013 International Union of Crystallography 2013-05-24 International Union of Crystallography International Union of Crystallography http://journals.iucr.org urn:issn:1744-3091 Acta Crystallographica Section F: Structural Biology and Crystallization Communications is a rapid all-electronic journal, which provides a home for short communications on the crystallization and structure of biological macromolecules. Structures determined through structural genomics initiatives or from iterative studies such as those used in the pharmaceutical industry are particularly welcomed. Articles are available online when ready, making publication as fast as possible, and include unlimited free colour illustrations, movies and other enhancements. The editorial process is completely electronic with respect to deposition, submission, refereeing and publication. text/html Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Volume 69, Part 6, 2013 text monthly 1 2002-01-01T00:00+00:00 6 69 2013-05-24 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications 472 urn:issn:1744-3091 med@iucr.org May 2013 2013-05-24 http://journals.iucr.org/logos/rss10f.gif http://journals.iucr.org/f/issues/2013/06/00/isscontsbdy.html Still image http://scripts.iucr.org/cgi-bin/paper?tz5026 Keap1 is a substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex and plays an important role in the cellular response to oxidative stress. It binds Nrf2 with its Kelch domain and thus triggers the ubiquitinylation and degradation of Nrf2. Oxidative stress prevents the degradation of Nrf2 and leads to the activation of cytoprotective genes. Therefore, Keap1 is an attractive drug target in inflammatory diseases. The support of a medicinal chemistry effort by structural research requires a robust crystallization system in which the crystals are preferably suited for performing soaking experiments. This facilitates the generation of protein–ligand complexes in a routine and high-throughput manner. The structure of human Keap1 has been described previously. In this crystal form, however, the binding site for Nrf2 was blocked by a crystal contact. This interaction was analysed and mutations were introduced to disrupt this crystal contact. One double mutation (E540A/E542A) crystallized in a new crystal form in which the binding site for Nrf2 was not blocked and was accessible to small-molecule ligands. The crystal structures of the apo form of the mutated Keap1 Kelch domain (1.98 Å resolution) and of the complex with an Nrf2-derived peptide obtained by soaking (2.20 Å resolution) are reported. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Hörer, S. Reinert, D. Ostmann, K. Hoevels, Y. Nar, H. 2013-05-23 doi:10.1107/S174430911301124X International Union of Crystallography A mutant of the Kelch domain of the human Keap1 protein has been designed in order to enable the soaking of small-molecule ligands. The apo structure of this mutant is reported at 1.98 Å resolution and the suitability of the crystal system has been demonstrated by the structure of the mutated Keap1 Kelch domain in complex with a cyclic peptide derived from Nrf2. EN Keap1 Kelch crystal contacts Keap1 is a substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex and plays an important role in the cellular response to oxidative stress. It binds Nrf2 with its Kelch domain and thus triggers the ubiquitinylation and degradation of Nrf2. Oxidative stress prevents the degradation of Nrf2 and leads to the activation of cytoprotective genes. Therefore, Keap1 is an attractive drug target in inflammatory diseases. The support of a medicinal chemistry effort by structural research requires a robust crystallization system in which the crystals are preferably suited for performing soaking experiments. This facilitates the generation of protein–ligand complexes in a routine and high-throughput manner. The structure of human Keap1 has been described previously. In this crystal form, however, the binding site for Nrf2 was blocked by a crystal contact. This interaction was analysed and mutations were introduced to disrupt this crystal contact. One double mutation (E540A/E542A) crystallized in a new crystal form in which the binding site for Nrf2 was not blocked and was accessible to small-molecule ligands. The crystal structures of the apo form of the mutated Keap1 Kelch domain (1.98 Å resolution) and of the complex with an Nrf2-derived peptide obtained by soaking (2.20 Å resolution) are reported. text/html Crystal-contact engineering to obtain a crystal form of the Kelch domain of human Keap1 suitable for ligand-soaking experiments text 6 69 2013-05-23 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 0 0 http://scripts.iucr.org/cgi-bin/paper?fw5406 Dibenzothiophene (DBT) and its derivatives are typical sulfur compounds found in fossil fuels. These compounds show resistance to the hydrodesulfurization treatment that is commonly used in industry. Dibenzothiophene monooxygenase (DszC) is responsible for the oxidation of DBT, which is the first and the rate-limiting step in the DBT enzymatic desulfurization 4S pathway. In this study, the crystal structure of DszC from Rhodococcus erythropolis DS-3 is reported. The crystal of native DszC belonged to space group P1, with unit-cell parameters a = 96.16, b = 96.27, c = 98.56 Å, α = 81.03, β = 67.57, γ = 85.84°. To determine the phase, SAD X-ray diffraction data were collected from a SeMet-derivative DszC crystal, which also belonged to space group P1, with unit-cell parameters a = 95.379, b = 95.167, c = 94.891 Å, α = 87.046, β = 70.536, γ = 79.738°. Further structural analysis of DszC is in progress. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Duan, X. Zhang, L. Zhou, D. Ji, K. Ma, T. Shui, W. Li, G. Li, X. 2013-05-23 doi:10.1107/S1744309113011172 International Union of Crystallography The structure of DszC from R. erythropolis DS-3 was solved using the single-wavelength anomalous dispersion method. EN DszC SAD Rhodococcus erythropolis Dibenzothiophene (DBT) and its derivatives are typical sulfur compounds found in fossil fuels. These compounds show resistance to the hydrodesulfurization treatment that is commonly used in industry. Dibenzothiophene monooxygenase (DszC) is responsible for the oxidation of DBT, which is the first and the rate-limiting step in the DBT enzymatic desulfurization 4S pathway. In this study, the crystal structure of DszC from Rhodococcus erythropolis DS-3 is reported. The crystal of native DszC belonged to space group P1, with unit-cell parameters a = 96.16, b = 96.27, c = 98.56 Å, α = 81.03, β = 67.57, γ = 85.84°. To determine the phase, SAD X-ray diffraction data were collected from a SeMet-derivative DszC crystal, which also belonged to space group P1, with unit-cell parameters a = 95.379, b = 95.167, c = 94.891 Å, α = 87.046, β = 70.536, γ = 79.738°. Further structural analysis of DszC is in progress. text/html Crystallization and preliminary structural analysis of dibenzothiophene monooxygenase (DszC) from Rhodococcus erythropolis text 6 69 2013-05-23 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 0 0 http://scripts.iucr.org/cgi-bin/paper?tt5039 The Gag precursor is the major structural protein of the virion of human immunodeficiency virus-1 (HIV-1). Capsid protein (CA), a cleavage product of Gag, plays an essential role in virus assembly both in Gag-precursor multimerization and in capsid core formation. The carboxy-terminal domain (CTD) of CA contains 20 residues that are highly conserved across retroviruses and constitute the major homology region (MHR). Genetic evidence implies a role for the MHR in interactions between Gag precursors during the assembly of the virus, but the structural basis for this role remains elusive. This paper describes a novel triclinic structure of the HIV-1 CA CTD at 1.6 Å resolution with two canonical dimers of CA CTD in the asymmetric unit. The canonical dimers form a newly identified packing interface where interactions of four conserved MHR residues take place. This is the first structural indication that these MHR residues participate in the putative CTD–CTD interactions. These findings suggest that the molecules forming this novel interface resemble an intermediate structure that participates in the early steps of HIV-1 assembly. This interface may therefore provide a novel target for antiviral drugs. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Lampel, A. Yaniv, O. Berger, O. Bacharach, E. Gazit, E. Frolow, F. 2013-05-23 doi:10.1107/S1744309113011871 International Union of Crystallography The triclinic structure of the HIV-1 capsid protein contains four molecules in the asymmetric unit that form a novel packing interface that could conceivably resemble an intermediate structure that is involved in the early steps of HIV-1 assembly. EN HIV-1 capsid protein Gag precursor The Gag precursor is the major structural protein of the virion of human immunodeficiency virus-1 (HIV-1). Capsid protein (CA), a cleavage product of Gag, plays an essential role in virus assembly both in Gag-precursor multimerization and in capsid core formation. The carboxy-terminal domain (CTD) of CA contains 20 residues that are highly conserved across retroviruses and constitute the major homology region (MHR). Genetic evidence implies a role for the MHR in interactions between Gag precursors during the assembly of the virus, but the structural basis for this role remains elusive. This paper describes a novel triclinic structure of the HIV-1 CA CTD at 1.6 Å resolution with two canonical dimers of CA CTD in the asymmetric unit. The canonical dimers form a newly identified packing interface where interactions of four conserved MHR residues take place. This is the first structural indication that these MHR residues participate in the putative CTD–CTD interactions. These findings suggest that the molecules forming this novel interface resemble an intermediate structure that participates in the early steps of HIV-1 assembly. This interface may therefore provide a novel target for antiviral drugs. text/html A triclinic crystal structure of the carboxy-terminal domain of HIV-1 capsid protein with four molecules in the asymmetric unit reveals a novel packing interface text 6 69 2013-05-23 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 0 0 http://scripts.iucr.org/cgi-bin/paper?sw5060 The type VI secretion system of Pseudomonas aeruginosa has been shown to be responsible for the translocation of bacteriolytic effectors into competing bacteria. A mechanistic understanding of this widely distributed secretion system is developing and structural studies of its components are ongoing. Two representative structures of one highly conserved component, TssJ, from Escherichia coli and Serratia marcescens have been published. Here, the X-ray crystal structure of TssJ1 from P. aeruginosa is presented at 1.4 Å resolution. The overall structure is conserved among the three proteins. This finding suggests that the homologues function in a similar manner and bolsters the understanding of the structure of this family of proteins. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Robb, C.S. Assmus, M. Nano, F.E. Boraston, A.B. 2013-05-23 doi:10.1107/S1744309113012220 International Union of Crystallography The crystal structure of the type VI secretion-system protein TssJ1 from P. aeruginosa was solved by iodide SAD at a resolution of 1.4 Å. EN T6SS lipoproteins Pseudomonas aeruginosa TssJ1 The type VI secretion system of Pseudomonas aeruginosa has been shown to be responsible for the translocation of bacteriolytic effectors into competing bacteria. A mechanistic understanding of this widely distributed secretion system is developing and structural studies of its components are ongoing. Two representative structures of one highly conserved component, TssJ, from Escherichia coli and Serratia marcescens have been published. Here, the X-ray crystal structure of TssJ1 from P. aeruginosa is presented at 1.4 Å resolution. The overall structure is conserved among the three proteins. This finding suggests that the homologues function in a similar manner and bolsters the understanding of the structure of this family of proteins. text/html Structure of the T6SS lipoprotein TssJ1 from Pseudomonas aeruginosa text 6 69 2013-05-23 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 0 0 http://scripts.iucr.org/cgi-bin/paper?sw5061 The bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase (RibD) represents a potential antibacterial drug target. The structure of recombinant Acinetobacter baumannii RibD is reported in orthorhombic and tetragonal crystal forms at 2.2 and 2.0 Å resolution, respectively. Comparisons with orthologous structures in the Protein Data Bank indicated close similarities. The tetragonal crystal form was obtained in the presence of guanosine monophosphate, which surprisingly was observed to occupy the adenine-binding site of the reductase domain. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Dawson, A. Trumper, P. Chrysostomou, G. Hunter, W.N. 2013-05-23 doi:10.1107/S174430911301292X International Union of Crystallography The structure of a bifunctional deaminase/reductase involved in riboflavin biosynthesis in the pathogen A. baumannii has been determined in two crystal forms. EN bifunctional deaminase/reductase Acinetobacter baumannii RibD riboflavin biosynthesis The bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase (RibD) represents a potential antibacterial drug target. The structure of recombinant Acinetobacter baumannii RibD is reported in orthorhombic and tetragonal crystal forms at 2.2 and 2.0 Å resolution, respectively. Comparisons with orthologous structures in the Protein Data Bank indicated close similarities. The tetragonal crystal form was obtained in the presence of guanosine monophosphate, which surprisingly was observed to occupy the adenine-binding site of the reductase domain. text/html Structure of diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase from Acinetobacter baumannii text 6 69 2013-05-23 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 0 0 http://scripts.iucr.org/cgi-bin/paper?gx5216 Patellamides are macrocyclic peptides with potent biological effects and are a subset of the cyanobactins. Cyanobactins are natural products that are produced by a series of enzymatic transformations and a common modification is the addition of a prenyl group. Puzzlingly, the pathway for patellamides in Prochloron didemni contains a gene, patF, with homology to prenylases, but patellamides are not themselves prenylated. The structure of the protein PatF was cloned, expressed, purified and determined. Prenylase activity could not be demonstrated for the protein, and examination of the structure revealed changes in side-chain identity at the active site. It is suggested that these changes have inactivated the protein. Attempts to mutate these residues led to unfolded protein. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Bent, A.F. Koehnke, J. Houssen, W.E. Smith, M.C.M. Jaspars, M. Naismith, J.H. 2013-05-23 doi:10.1107/S1744309113012931 International Union of Crystallography The X-ray crystal structure of PatF from P. didemni was solved by the single-wavelength anomalous diffraction method to a resolution of 2.13 Å. EN patellamide cyanobactins natural products prenyltransferases Patellamides are macrocyclic peptides with potent biological effects and are a subset of the cyanobactins. Cyanobactins are natural products that are produced by a series of enzymatic transformations and a common modification is the addition of a prenyl group. Puzzlingly, the pathway for patellamides in Prochloron didemni contains a gene, patF, with homology to prenylases, but patellamides are not themselves prenylated. The structure of the protein PatF was cloned, expressed, purified and determined. Prenylase activity could not be demonstrated for the protein, and examination of the structure revealed changes in side-chain identity at the active site. It is suggested that these changes have inactivated the protein. Attempts to mutate these residues led to unfolded protein. text/html Structure of PatF from Prochloron didemni text 6 69 2013-05-23 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 0 0 http://scripts.iucr.org/cgi-bin/paper?kw5066 Borrelia burgdorferi is a spirochete responsible for Lyme disease, the most commonly occurring vector-borne disease in Europe and North America. The bacterium utilizes a set of proteins, termed complement regulator-acquiring surface proteins (CRASPs), to aid evasion of the human complement system by recruiting and presenting complement regulator factor H on its surface in a manner that mimics host cells. Presented here is the atomic resolution structure of a member of this protein family, ErpC. The structure provides new insights into the mechanism of recruitment of factor H and other factor H-related proteins by acting as a molecular mimic of host glycosaminoglycans. It also describes the architecture of other CRASP proteins belonging to the OspE/F-related paralogous protein family and suggests that they have evolved to bind specific complement proteins, aiding survival of the bacterium in different hosts. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Caesar, J.J.E. Johnson, S. Kraiczy, P. Lea, S.M. 2013-05-23 doi:10.1107/S1744309113013249 International Union of Crystallography The structure of ErpC, a member of the complement regulator-acquiring surface protein family from B. burgdorferi, has been solved, providing insights into the strategies of complement evasion by this zoonotic bacterium and suggesting a common architecture for other members of this protein family. EN BbCRASP-4 Borrelia burgdorferi ErpC factor H complement Borrelia burgdorferi is a spirochete responsible for Lyme disease, the most commonly occurring vector-borne disease in Europe and North America. The bacterium utilizes a set of proteins, termed complement regulator-acquiring surface proteins (CRASPs), to aid evasion of the human complement system by recruiting and presenting complement regulator factor H on its surface in a manner that mimics host cells. Presented here is the atomic resolution structure of a member of this protein family, ErpC. The structure provides new insights into the mechanism of recruitment of factor H and other factor H-related proteins by acting as a molecular mimic of host glycosaminoglycans. It also describes the architecture of other CRASP proteins belonging to the OspE/F-related paralogous protein family and suggests that they have evolved to bind specific complement proteins, aiding survival of the bacterium in different hosts. text/html ErpC, a member of the complement regulator-acquiring family of surface proteins from Borrelia burgdorferi, possesses an architecture previously unseen in this protein family text 6 69 2013-05-23 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 0 0 http://scripts.iucr.org/cgi-bin/paper?tb5057 Borrelia burgdorferi has evolved many mechanisms of evading the different immune systems across its range of reservoir hosts, including the capture and presentation of host complement regulators factor H and factor H-like protein-1 (FHL-1). Acquisition is mediated by a family of complement regulator-acquiring surface proteins (CRASPs), of which the atomic structure of CspA (BbCRASP-1) is known and shows the formation of a homodimeric species which is required for binding. Mutagenesis studies have mapped a putative factor H binding site to a cleft between the two subunits. Presented here is a new atomic structure of CspA which shows a degree of flexibility between the subunits which may be critical for factor H scavenging by increasing access to the binding interface and allows the possibility that the assembly can clamp around the bound complement regulators. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Caesar, J.J.E. Wallich, R. Kraiczy, P. Zipfel, P.F. Lea, S.M. 2013-05-23 doi:10.1107/S1744309113012748 International Union of Crystallography B. burgdorferi binds complement factor H using a dimeric surface protein, CspA (BbCRASP-1). Presented here is a new structure of CspA that suggests that there is a degree of flexibility between subunits which may have implications for complement regulator binding. EN complement factor H BbCRASP-1 CspA Borrelia burgdorferi Borrelia burgdorferi has evolved many mechanisms of evading the different immune systems across its range of reservoir hosts, including the capture and presentation of host complement regulators factor H and factor H-like protein-1 (FHL-1). Acquisition is mediated by a family of complement regulator-acquiring surface proteins (CRASPs), of which the atomic structure of CspA (BbCRASP-1) is known and shows the formation of a homodimeric species which is required for binding. Mutagenesis studies have mapped a putative factor H binding site to a cleft between the two subunits. Presented here is a new atomic structure of CspA which shows a degree of flexibility between the subunits which may be critical for factor H scavenging by increasing access to the binding interface and allows the possibility that the assembly can clamp around the bound complement regulators. text/html Further structural insights into the binding of complement factor H by complement regulator-acquiring surface protein 1 (CspA) of Borrelia burgdorferi text 6 69 2013-05-23 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 0 0 http://scripts.iucr.org/cgi-bin/paper?tz5032 In the course of a crystallographic study of a 132 nt variant of Aquifex aeolicus 6S RNA, a crystal structure of an A-form RNA duplex containing 12 base pairs was solved at a resolution of 2.6 Å. In fact, the RNA duplex is part of the 6S RNA and was obtained by accidental but precise degradation of the 6S RNA in a crystallization droplet. 6S RNA degradation was confirmed by microscopic observation of crystals and gel electrophoresis of crystallization droplets. The RNA oligomers obtained form regular A-form duplexes containing three GoU wobble-type base pairs, one of which engages in intermolecular contacts through a ribose-zipper motif at the crystal-packing interface. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Kondo, J. Dock-Bregeon, A.-C. Willkomm, D.K. Hartmann, R.K. Westhof, E. 2013-05-24 doi:10.1107/S1744309113013018 International Union of Crystallography The crystal structure of an A-form RNA duplex obtained by degradation of 6S RNA in a crystallization droplet has been solved. The role of a ribose zipper motif in the intermolecular packing is presented. EN A-form RNA 6S RNA RNA degradation In the course of a crystallographic study of a 132 nt variant of Aquifex aeolicus 6S RNA, a crystal structure of an A-form RNA duplex containing 12 base pairs was solved at a resolution of 2.6 Å. In fact, the RNA duplex is part of the 6S RNA and was obtained by accidental but precise degradation of the 6S RNA in a crystallization droplet. 6S RNA degradation was confirmed by microscopic observation of crystals and gel electrophoresis of crystallization droplets. The RNA oligomers obtained form regular A-form duplexes containing three GoU wobble-type base pairs, one of which engages in intermolecular contacts through a ribose-zipper motif at the crystal-packing interface. text/html Structure of an A-form RNA duplex obtained by degradation of 6S RNA in a crystallization droplet text 6 69 2013-05-24 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 0 0 http://scripts.iucr.org/cgi-bin/paper?hc5157 RlmM is an AdoMet-dependent methyltransferase that is responsible for 2′-O-methylation of C2498 in the peptidyl-transferase loop of bacterial 23S rRNA. This modification occurs before assembly of the 50S ribosomal subunit, and lack of C2498 methylation can cause a slight reduction in bacterial fitness. Here, the purification and crystallization of RlmM from Escherichia coli as well as its preliminary crystallographic analysis are presented. Cocrystallization of RlmM with AdoMet was carried out and X-ray diffraction data were collected to a resolution of 2.30 Å on beamline BL17U at the SSRF. However, electron density for AdoMet cannot be observed by comprehensive crystallographic analysis, indicating that it is not bound by RlmM during the cocrystallization process. The structure was solved by molecular replacement and refinement is in progress. The crystal contained one molecule in the asymmetric unit and belonged to space group P21, with unit-cell parameters a = 56.07, b = 59.38, c = 54.35 Å, β = 94.84°, which differs from the P31 or P3121 space groups of previously reported RlmM structures (PDB entries 4auk, 4atn and 4b17). Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Guo, H.-Y. Gao, Z.-Q. Zhang, H. Wei, Y. Xu, J.-H. Wang, W. Yan, A. Dong, Y.-H. 2013-05-24 doi:10.1107/S1744309113006611 International Union of Crystallography The crystal of Escherichia coli 23S rRNA methyltransferase RlmM in this study belongs to a new space group (P21) and is different from the known P31 or P3121 space groups. EN RNA modification methyltransferases RlmM AdoMet RlmM is an AdoMet-dependent methyltransferase that is responsible for 2′-O-methylation of C2498 in the peptidyl-transferase loop of bacterial 23S rRNA. This modification occurs before assembly of the 50S ribosomal subunit, and lack of C2498 methylation can cause a slight reduction in bacterial fitness. Here, the purification and crystallization of RlmM from Escherichia coli as well as its preliminary crystallographic analysis are presented. Cocrystallization of RlmM with AdoMet was carried out and X-ray diffraction data were collected to a resolution of 2.30 Å on beamline BL17U at the SSRF. However, electron density for AdoMet cannot be observed by comprehensive crystallographic analysis, indicating that it is not bound by RlmM during the cocrystallization process. The structure was solved by molecular replacement and refinement is in progress. The crystal contained one molecule in the asymmetric unit and belonged to space group P21, with unit-cell parameters a = 56.07, b = 59.38, c = 54.35 Å, β = 94.84°, which differs from the P31 or P3121 space groups of previously reported RlmM structures (PDB entries 4auk, 4atn and 4b17). text/html Purification, crystallization and preliminary crystallographic analysis of the 23S rRNA methyltransferase RlmM (Cm2498) from Escherichia coli text 6 69 2013-05-24 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?dp5046 Long-term nonprogression during simian immunodeficiency virus (SIV) infection has been strongly associated with the major histocompatibility complex (MHC) class I allele Mamu-B*17. Here, a complex of rhesus macaque Mamu-B*17 with rhesus macaque β2-microglobulin (β2m) and an immunodominant peptide (SIVmac239 Env241–251; LRCNDTNYSGF; Env LF11) derived from the SIV Env protein was crystallized by the hanging-drop method using PEG 3350 as a precipitating agent. The crystals belonged to the primitive monoclinic space group P2, with unit-cell parameters a = 68.3, b = 45.0, c = 81.5 Å, β = 96.5°. Assuming the presence of one molecule in the asymmetric unit, the Matthews coefficient and solvent content were calculated to be 2.96 Å3 Da−1 and 58.5%, respectively. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Gao, F. Bao, J. 2013-05-24 doi:10.1107/S1744309113011251 International Union of Crystallography A primitive monoclinic crystal of the rhesus macaque MHC class I molecule Mamu-B*17 complexed with an SIVmac239 Env peptide was obtained and belonged to space group P2, with unit-cell parameters a = 68.3, b = 45.0, c = 81.5 Å, β = 96.5°. The crystal diffracted to 2.55 Å resolution. EN elite controllers MHC rhesus macaque SIV Long-term nonprogression during simian immunodeficiency virus (SIV) infection has been strongly associated with the major histocompatibility complex (MHC) class I allele Mamu-B*17. Here, a complex of rhesus macaque Mamu-B*17 with rhesus macaque β2-microglobulin (β2m) and an immunodominant peptide (SIVmac239 Env241–251; LRCNDTNYSGF; Env LF11) derived from the SIV Env protein was crystallized by the hanging-drop method using PEG 3350 as a precipitating agent. The crystals belonged to the primitive monoclinic space group P2, with unit-cell parameters a = 68.3, b = 45.0, c = 81.5 Å, β = 96.5°. Assuming the presence of one molecule in the asymmetric unit, the Matthews coefficient and solvent content were calculated to be 2.96 Å3 Da−1 and 58.5%, respectively. text/html Crystallization and preliminary X-ray crystallographic analysis of the rhesus macaque MHC class I molecule Mamu-B*17 complexed with an immunodominant SIVmac239 Env epitope text 6 69 2013-05-24 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?en5534 An osmotin (CpOsm) from the latex of Calotropis procera has been crystallized in both tetragonal and trigonal forms suitable for structure determination. Crystallographic studies of CpOsm are of great interest because limited information is available concerning the structure of latex proteins and CpOsm has previously been shown to interact with the spore membranes of some plant pathogenic fungi, thus impairing spore germination and hyphal growth. CpOsm crystals were grown using 0.1 M HEPES buffer pH 7.5, 26% PEG 4000, 0.2 M ammonium sulfate (space group P43) or using 0.1 M HEPES buffer pH 7.5, 35% MPD, 0.7 M ammonium sulfate (space group P3112). X-ray diffraction data were collected to 2.17 Å (P43) and 1.80 Å (P3112) resolution and molecular-replacement analyses produced initial phases for both crystal forms. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Bruno-Moreno, F. Sombra Basílio de Oliveira, R. de Azevedo Moreira, R. Pinto Lobo, M.D. Teixeira de Freitas, C.D. Viana Ramos, M. Barbosa Grangeiro, T. Oliveira Monteiro-Moreira, A.C. 2013-05-24 doi:10.1107/S1744309113011378 International Union of Crystallography An osmotin from the latex of Calotropis procera has been crystallized in both tetragonal and trigonal forms suitable for structure determination. EN Calotropis procera latex proteins osmotins PR-5 thaumatin-like proteins An osmotin (CpOsm) from the latex of Calotropis procera has been crystallized in both tetragonal and trigonal forms suitable for structure determination. Crystallographic studies of CpOsm are of great interest because limited information is available concerning the structure of latex proteins and CpOsm has previously been shown to interact with the spore membranes of some plant pathogenic fungi, thus impairing spore germination and hyphal growth. CpOsm crystals were grown using 0.1 M HEPES buffer pH 7.5, 26% PEG 4000, 0.2 M ammonium sulfate (space group P43) or using 0.1 M HEPES buffer pH 7.5, 35% MPD, 0.7 M ammonium sulfate (space group P3112). X-ray diffraction data were collected to 2.17 Å (P43) and 1.80 Å (P3112) resolution and molecular-replacement analyses produced initial phases for both crystal forms. text/html Crystallization and X-ray diffraction analysis of an antifungal laticifer protein text 6 69 2013-05-24 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?no5016 AAL-2 is a recently discovered lectin from the mushroom Agrocybe aegerita that specifically recognizes nonreducing terminal acetylglucosamine (GlcNAc) and that could be used as a probe in studies of protein O-linked β-N-acetylglucosamination (O-GlyNAcylation). In order to illustrate the mechanism of how this protein specifically recognizes nonreducing terminal GlcNAc and to evaluate the efficacy of AAL-2 as a macromolecular probe in O-GlyNAcylation studies, expression and crystallization studies of AAL-2 were performed and a diffraction data set was collected to 2.0 Å resolution. Preliminary crystallographic studies revealed that the AAL-2 crystals belonged to space group P212121, with unit-cell parameters a = 52.60, b = 111.70, c = 135.97 Å. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Ren, X. Jiang, S. Li, D. Sun, H. Wang, D. 2013-05-24 doi:10.1107/S1744309113011639 International Union of Crystallography AAL-2, an A. aegerita lectin that specifically recognizes nonreducing terminal acetylglucosamine, was crystallized and preliminary crystallographic studies were performed on this protein. This work provides a solid foundation for determination of the AAL-2 structure and illustration of the sugar-binding specificity of this novel lectin. EN AAL-2 lectin nonreducing terminal N-acetylglucosamine O-GlcNAcylation AAL-2 is a recently discovered lectin from the mushroom Agrocybe aegerita that specifically recognizes nonreducing terminal acetylglucosamine (GlcNAc) and that could be used as a probe in studies of protein O-linked β-N-acetylglucosamination (O-GlyNAcylation). In order to illustrate the mechanism of how this protein specifically recognizes nonreducing terminal GlcNAc and to evaluate the efficacy of AAL-2 as a macromolecular probe in O-GlyNAcylation studies, expression and crystallization studies of AAL-2 were performed and a diffraction data set was collected to 2.0 Å resolution. Preliminary crystallographic studies revealed that the AAL-2 crystals belonged to space group P212121, with unit-cell parameters a = 52.60, b = 111.70, c = 135.97 Å. text/html Crystallization and preliminary crystallographic studies of AAL-2, a novel lectin from Agrocybe aegerita that binds nonreducing terminal N-acetylglucosamine text 6 69 2013-05-24 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?pu5392 Acinetobacter baumannii is a virulent pathogenic bacterium that is resistant to most currently available antibiotics. Therefore, the design of drugs for the treatment of infections caused by A. baumannii is urgently required. Dihydrodipicolinate reductase (DHDPR) is an important enzyme which is involved in the biosynthetic pathway that leads to the production of l-lysine in bacteria. In order to design potent inhibitors against this enzyme, its detailed three-dimensional structure is required. DHDPR from A. baumannii (AbDHDPR) has been cloned, expressed, purified and crystallized. Here, the preliminary X-ray crystallographic data of AbDHDPR are reported. The crystals were grown using the hanging-drop vapour-diffusion method with PEG 3350 as the precipitating agent The crystals belonged to the orthorhombic space group P222, with unit-cell parameters a = 80.0, b = 100.8, c = 147.6 Å, and contained four molecules in the asymmetric unit. The complete structure determination of AbDHDPR is in progress. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Kaushik, S. Singh, A. Sinha, M. Kaur, P. Sharma, S. Singh, T.P. 2013-05-24 doi:10.1107/S1744309113011214 International Union of Crystallography Dihydrodipicolinate reductase has been cloned, expressed and crystallized. The crystals belong to orthorhombic space group P222, with unit-cell parameters a = 80.0, b = 100.8, c = 147.6 Å. EN dihydrodipicolinate reductase Acinetobacter baumannii lysine biosynthesis Acinetobacter baumannii is a virulent pathogenic bacterium that is resistant to most currently available antibiotics. Therefore, the design of drugs for the treatment of infections caused by A. baumannii is urgently required. Dihydrodipicolinate reductase (DHDPR) is an important enzyme which is involved in the biosynthetic pathway that leads to the production of l-lysine in bacteria. In order to design potent inhibitors against this enzyme, its detailed three-dimensional structure is required. DHDPR from A. baumannii (AbDHDPR) has been cloned, expressed, purified and crystallized. Here, the preliminary X-ray crystallographic data of AbDHDPR are reported. The crystals were grown using the hanging-drop vapour-diffusion method with PEG 3350 as the precipitating agent The crystals belonged to the orthorhombic space group P222, with unit-cell parameters a = 80.0, b = 100.8, c = 147.6 Å, and contained four molecules in the asymmetric unit. The complete structure determination of AbDHDPR is in progress. text/html Cloning, expression, crystallization and preliminary structural studies of dihydrodipicolinate reductase from Acinetobacter baumannii text 6 69 2013-05-24 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?hc5160 GluB is a substrate-binding protein (SBP) which participates in the uptake of glutamic acid in Corynebacterium glutamicum, a Gram-positive bacterium. It is part of an ATP-binding cassette (ABC) transporter system. Together with the transmembrane proteins GluC and GluD and the cytoplasmic protein GluA, which couples the hydrolysis of ATP to the translocation of glutamate, they form a highly active glutamate-uptake system. As part of efforts to study the amino-acid metabolism, especially the metabolism of glutamic acid by C. glutamicum, a bacterium that is widely used in the industrial production of glutamic acid, the GluB protein was expressed, purified and crystallized, an X-ray diffraction data set was collected to a resolution of 1.9 Å and preliminary crystallographic analysis was performed. The crystal belonged to space group P3121 or P3221, with unit-cell parameters a = b = 82.50, c = 72.69 Å. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Liu, Q. Li, D. Hu, Y. Wang, D.-C. 2013-05-25 doi:10.1107/S1744309113011652 International Union of Crystallography GluB, a substrate-binding protein from C. glutamicum, was expressed, purified and crystallized, followed by X-ray diffraction data collection and preliminary crystallographic analysis. EN Corynebacterium glutamicum glutamic acid binding protein glutamic acid metabolism GluB is a substrate-binding protein (SBP) which participates in the uptake of glutamic acid in Corynebacterium glutamicum, a Gram-positive bacterium. It is part of an ATP-binding cassette (ABC) transporter system. Together with the transmembrane proteins GluC and GluD and the cytoplasmic protein GluA, which couples the hydrolysis of ATP to the translocation of glutamate, they form a highly active glutamate-uptake system. As part of efforts to study the amino-acid metabolism, especially the metabolism of glutamic acid by C. glutamicum, a bacterium that is widely used in the industrial production of glutamic acid, the GluB protein was expressed, purified and crystallized, an X-ray diffraction data set was collected to a resolution of 1.9 Å and preliminary crystallographic analysis was performed. The crystal belonged to space group P3121 or P3221, with unit-cell parameters a = b = 82.50, c = 72.69 Å. text/html Expression, crystallization and preliminary crystallographic study of GluB from Corynebacterium glutamicum text 6 69 2013-05-25 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?nj5153 Alanine racemase (AlrMB4), a dimeric PLP-dependent thermostable enzyme from the anaerobic eubacterium Thermoanaerobacter tengcongensis MB4, was expressed and purified with a His6 tag in a form suitable for X-ray crystallographic analysis. Crystals were grown by the hanging-drop vapour-diffusion method at 289 K using a solution consisting of 0.1 M bis-tris pH 7.0, 22%(w/v) polyethylene glycol 4000. X-ray diffraction data were collected to 2.6 Å resolution. The crystal belonged to the orthorhombic space group P212121, with two protein molecules in an asymmetric unit. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Dong, H. Xu, S. Lu, X. He, G. Zhao, R. Chen, S. Fu, S. Ju, J. 2013-05-25 doi:10.1107/S1744309113011743 International Union of Crystallography A thermostable alanine racemase from T. tengcongensis MB4 was expressed in E. coli and purified. Crystallization and preliminary X-ray crystallographic analysis were performed for the recombinant enzyme. EN Thermoanaerobacter tengcongensis alanine racemase Alanine racemase (AlrMB4), a dimeric PLP-dependent thermostable enzyme from the anaerobic eubacterium Thermoanaerobacter tengcongensis MB4, was expressed and purified with a His6 tag in a form suitable for X-ray crystallographic analysis. Crystals were grown by the hanging-drop vapour-diffusion method at 289 K using a solution consisting of 0.1 M bis-tris pH 7.0, 22%(w/v) polyethylene glycol 4000. X-ray diffraction data were collected to 2.6 Å resolution. The crystal belonged to the orthorhombic space group P212121, with two protein molecules in an asymmetric unit. text/html Crystallization and preliminary X-ray study of a thermostable alanine racemase from Thermoanaerobacter tengcongensis MB4 text 6 69 2013-05-25 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?pg5015 In Escherichia coli and Salmonella enterica, bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP), a ubiquitous bacterial second-messenger molecule that participates in many cellular processes, can regulate flagellar motor speed and reduce cell swimming velocity by binding to the PilZ-containing protein YcgR. Here, the crystallization and preliminary X-ray crystallographic analysis of YcgR with c-di-GMP are reported. The crystals diffracted to 2.3 Å resolution and belonged to space group R3:H, with unit-cell parameters a = b = 93.96, c = 109.61 Å. The asymmetric unit appeared to contain one subunit with a Matthews coefficient of 3.21 Å3 Da−1. The results reported here provide a sound basis for solving the crystal structure of YcgR with c-di-GMP and revealing its structure–function relationship based on the three-dimensional structure. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Hou, Y. Li, D.-F. Wang, D.-C. 2013-05-25 doi:10.1107/S1744309113011937 International Union of Crystallography The flagellar motor `brake' protein YcgR from E. coli was crystallized with c-di-GMP. The crystals diffracted to 2.3 Å resolution and belonged to space group R3:H, with unit-cell parameters a = b = 93.96, c = 109.61 Å. EN Escherichia coli flagellar motility regulation c-di-GMP binding protein YcgR In Escherichia coli and Salmonella enterica, bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP), a ubiquitous bacterial second-messenger molecule that participates in many cellular processes, can regulate flagellar motor speed and reduce cell swimming velocity by binding to the PilZ-containing protein YcgR. Here, the crystallization and preliminary X-ray crystallographic analysis of YcgR with c-di-GMP are reported. The crystals diffracted to 2.3 Å resolution and belonged to space group R3:H, with unit-cell parameters a = b = 93.96, c = 109.61 Å. The asymmetric unit appeared to contain one subunit with a Matthews coefficient of 3.21 Å3 Da−1. The results reported here provide a sound basis for solving the crystal structure of YcgR with c-di-GMP and revealing its structure–function relationship based on the three-dimensional structure. text/html Crystallization and preliminary X-ray analysis of the flagellar motor `brake' molecule YcgR with c-di-GMP from Escherichia coli text 6 69 2013-05-25 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?bo5120 The flavoenzyme fructosyl peptide oxidase (FPOX) catalyses the oxidative deglycation of fructosyl amino acids or fructosyl dipeptides to produce amino acids, glucosone and hydrogen peroxide. In this study, FPOX protein from Eupenicillium terrenum sp. (EtFPOX) was expressed in Escherichia coli and purified by Ni-affinity and gel-filtration chromatography. EtFPOX crystals were obtained using the sitting-drop vapour-diffusion method with polyethylene glycol 3350 as precipitant. X-ray diffraction data were collected to 1.90 Å resolution using a synchrotron-radiation source. The crystals belonged to space group P212121, with unit-cell parameters a = 65.6, b = 80.0, c = 83.4 Å, and contained one molecule in the asymmetric unit. The calculated Matthews coefficient and solvent content were 2.22 Å3 Da−1 and 44.62%, respectively. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Xing, K. Gan, W. Jia, M. Gao, F. Gong, W. 2013-05-25 doi:10.1107/S1744309113012128 International Union of Crystallography Crystals of EtFPOX from E. terrenum sp. diffracted to 1.9 Å resolution and belonged to space group P212121, with unit-cell parameters a = 65.6, b = 80.0, c = 83.4 Å. EN FPOX EtFPOX Eupenicillium terrenum sp. The flavoenzyme fructosyl peptide oxidase (FPOX) catalyses the oxidative deglycation of fructosyl amino acids or fructosyl dipeptides to produce amino acids, glucosone and hydrogen peroxide. In this study, FPOX protein from Eupenicillium terrenum sp. (EtFPOX) was expressed in Escherichia coli and purified by Ni-affinity and gel-filtration chromatography. EtFPOX crystals were obtained using the sitting-drop vapour-diffusion method with polyethylene glycol 3350 as precipitant. X-ray diffraction data were collected to 1.90 Å resolution using a synchrotron-radiation source. The crystals belonged to space group P212121, with unit-cell parameters a = 65.6, b = 80.0, c = 83.4 Å, and contained one molecule in the asymmetric unit. The calculated Matthews coefficient and solvent content were 2.22 Å3 Da−1 and 44.62%, respectively. text/html Expression, purification, crystallization and preliminary X-ray diffraction analysis of EtFPOX from Eupenicillium terrenum sp. text 6 69 2013-05-25 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?ub5046 Here, the crystallization and preliminary X-ray diffraction studies of Bacillus licheniformis γ-glutamyl transpeptidase (BlGT) are reported. The serendipitous finding of heterogeneous nucleants in the initial experiments provided the first crystallization conditions for the protein. Crystals were grown by hanging-drop vapour diffusion using a precipitant solution consisting of 20%(w/v) PEG 3350, 0.2 M magnesium chloride hexahydrate, 0.1 M Tris–HCl pH 8.2. The protein crystallized in the orthorhombic space group P212121, with one heterodimer per asymmetric unit and unit-cell parameters a = 60.90, b = 61.97, c = 148.24 Å. The BlGT crystals diffracted to 2.95 Å resolution. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Lin, L.-L. Merlino, A. 2013-05-25 doi:10.1107/S1744309113012165 International Union of Crystallography An additional example in which heterogeneous nucleation has helped in the search for crystallization conditions of a protein is reported. Optimization of the crystallization conditions led to the formation of single crystals of γ-glutamyl transpeptidase from B. licheniformis that diffracted to about 3.0 Å resolution. EN γ-glutamyl transpeptidase Bacillus licheniformis Here, the crystallization and preliminary X-ray diffraction studies of Bacillus licheniformis γ-glutamyl transpeptidase (BlGT) are reported. The serendipitous finding of heterogeneous nucleants in the initial experiments provided the first crystallization conditions for the protein. Crystals were grown by hanging-drop vapour diffusion using a precipitant solution consisting of 20%(w/v) PEG 3350, 0.2 M magnesium chloride hexahydrate, 0.1 M Tris–HCl pH 8.2. The protein crystallized in the orthorhombic space group P212121, with one heterodimer per asymmetric unit and unit-cell parameters a = 60.90, b = 61.97, c = 148.24 Å. The BlGT crystals diffracted to 2.95 Å resolution. text/html Heterogeneous nucleation helps the search for initial crystallization conditions of γ-glutamyl transpeptidase from Bacillus licheniformis text 6 69 2013-05-25 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?fw5405 Hyaluronate lyase is an important surface enzyme of many streptococcal species. The enzyme degrades several biologically important connective tissue components, which facilitates the spreading of the bacteria throughout the host tissues and presumably provides energy and a carbon source for bacterial cells. Recombinant hyaluronate lyase was expressed in Escherichia coli and was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to space group P2221, with unit-cell parameters a = 58.08, b = 101.32, c = 103.47 Å and one molecule in the asymmetric unit. Diffraction data were collected to 2.50 Å resolution. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Khan, A.H. Mohamed Omar, Y.M. Kakar, M.A. Bangulzai, N. 2013-05-25 doi:10.1107/S1744309113012554 International Union of Crystallography The cloning, expression, purification and crystallization of hyaluronate lyase enzyme from Streptococcus suis, are reported. EN hyaluronate lyase Streptococcus suis Hyaluronate lyase is an important surface enzyme of many streptococcal species. The enzyme degrades several biologically important connective tissue components, which facilitates the spreading of the bacteria throughout the host tissues and presumably provides energy and a carbon source for bacterial cells. Recombinant hyaluronate lyase was expressed in Escherichia coli and was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to space group P2221, with unit-cell parameters a = 58.08, b = 101.32, c = 103.47 Å and one molecule in the asymmetric unit. Diffraction data were collected to 2.50 Å resolution. text/html Crystallization and preliminary crystallographic analysis of recombinant hyaluronate lyase from Streptococcus suis text 6 69 2013-05-25 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?fw5410 Xyloglucanases (Xghs) are important enzymes involved in xyloglucan modification and degradation. Xanthomonas campestris pv. campestris (Xcc) is a phytopathogenic bacterium which produces a large number of glycosyl hydrolases (GH), but has only one family 74 GH (Xcc-Xgh). This enzyme was overexpressed in Escherichia coli, purified and crystallized. Diffraction data sets were collected for the native enzyme and its complex with glucose to maximum resolutions of 2.0 and 2.1 Å, respectively. The data were indexed in a hexagonal crystal system with unit-cell parameters a = b = 153.4, c = 84.9 Å. As indicated by molecular-replacement solution, the crystals belonged to space group P61. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 de Araújo, E.A. Tomazini, A. Kadowaki, M.A.S. Murakami, M.T. Polikarpov, I. 2013-05-25 doi:10.1107/S174430911301275X International Union of Crystallography X. campestris pv. campestris xyloglucanase was produced in E. coli using recombinant pSMT3 vector. Crystals were obtained and X-ray data sets were collected for both the apoenzyme and its complex with glucose. EN xyloglucanase GH74 family Xanthomonas campestris pv. campestris Xyloglucanases (Xghs) are important enzymes involved in xyloglucan modification and degradation. Xanthomonas campestris pv. campestris (Xcc) is a phytopathogenic bacterium which produces a large number of glycosyl hydrolases (GH), but has only one family 74 GH (Xcc-Xgh). This enzyme was overexpressed in Escherichia coli, purified and crystallized. Diffraction data sets were collected for the native enzyme and its complex with glucose to maximum resolutions of 2.0 and 2.1 Å, respectively. The data were indexed in a hexagonal crystal system with unit-cell parameters a = b = 153.4, c = 84.9 Å. As indicated by molecular-replacement solution, the crystals belonged to space group P61. text/html Crystallization and preliminary X-ray diffraction analysis of a new xyloglucanase from Xanthomonas campestris pv. campestris text 6 69 2013-05-25 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?fw5411 Mycobacterium tuberculosis DNA gyrase, a nanomachine involved in the regulation of DNA topology, is the only type II topoisomerase present in this organism and hence is the sole target of fluoroquinolones in the treatment of tuberculosis. The ATPase domain provides the energy required for catalysis by ATP hydrolysis. Two constructs corresponding to this 43 kDa domain, Mtb-GyrB47C1 and Mtb-GyrB47C2, have been overproduced, purified and crystallized. Diffraction data were collected from three crystal forms. The crystals belonged to space groups P1 and P21 and diffracted to resolutions of 2.9 and 3.3 Å, respectively. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Roué, M. Agrawal, A. Volker, C. Mossakowska, D. Mayer, C. Bax, B.D. 2013-05-25 doi:10.1107/S1744309113012906 International Union of Crystallography The ATPase domain of M. tuberculosis DNA gyrase was crystallized using hanging-drop vapour diffusion. The crystals belonged to space groups P1 and P21. Diffraction data were collected to resolutions of 2.9 and 3.3 Å, respectively. EN Mycobacterium tuberculosis type II topoisomerase DNA gyrase ATPase domain Mycobacterium tuberculosis DNA gyrase, a nanomachine involved in the regulation of DNA topology, is the only type II topoisomerase present in this organism and hence is the sole target of fluoroquinolones in the treatment of tuberculosis. The ATPase domain provides the energy required for catalysis by ATP hydrolysis. Two constructs corresponding to this 43 kDa domain, Mtb-GyrB47C1 and Mtb-GyrB47C2, have been overproduced, purified and crystallized. Diffraction data were collected from three crystal forms. The crystals belonged to space groups P1 and P21 and diffracted to resolutions of 2.9 and 3.3 Å, respectively. text/html Purification, crystallization and preliminary X-ray crystallographic studies of the Mycobacterium tuberculosis DNA gyrase ATPase domain text 6 69 2013-05-25 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?nj5155 Haloalkane dehalogenases are hydrolytic enzymes with a broad range of potential practical applications such as biodegradation, biosensing, biocatalysis and cellular imaging. Two newly isolated psychrophilic haloalkane dehalogenases exhibiting interesting catalytic properties, DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17, were purified and used for crystallization experiments. After the optimization of crystallization conditions, crystals of diffraction quality were obtained. Diffraction data sets were collected for native enzymes and complexes with selected ligands such as 1-bromohexane and 1,2-dichloroethane to resolutions ranging from 1.05 to 2.49 Å. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Tratsiak, K. Degtjarik, O. Drienovska, I. Chrast, L. Rezacova, P. Kuty, M. Chaloupkova, R. Damborsky, J. Kuta Smatanova, I. 2013-05-25 doi:10.1107/S1744309113012979 International Union of Crystallography The novel haloalkane dehalogenases DpcA from P. cryohalolentis K5 and DmxA from Marinobacter sp. ELB17 were successfully crystallized and diffraction data were collected to resolutions of 1.05 and 2.49 Å, respectively. EN haloalkane dehalogenases DpcA Psychrobacter cryohalolentis K5 DmxA Marinobacter sp. ELB17 Haloalkane dehalogenases are hydrolytic enzymes with a broad range of potential practical applications such as biodegradation, biosensing, biocatalysis and cellular imaging. Two newly isolated psychrophilic haloalkane dehalogenases exhibiting interesting catalytic properties, DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17, were purified and used for crystallization experiments. After the optimization of crystallization conditions, crystals of diffraction quality were obtained. Diffraction data sets were collected for native enzymes and complexes with selected ligands such as 1-bromohexane and 1,2-dichloroethane to resolutions ranging from 1.05 to 2.49 Å. text/html Crystallographic analysis of new psychrophilic haloalkane dehalogenases: DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17 text 6 69 2013-05-25 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0 http://scripts.iucr.org/cgi-bin/paper?nj5156 SaeR is the response regulator of the SaeRS two-component signal transduction system, which is involved in regulating bacterial autolysis and biofilm formation. SaeR comprises an N-terminal receiver domain and a C-terminal effector domain. The effector domain possesses DNA-binding and transactivation functions. Here, the effector domain of SaeR from Staphylococcus epidermidis was purified and crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 2.15 Å and belonged to space group P212121, with unit-cell parameters a = 34.20, b = 53.78, c = 111.66 Å. Determining the structure will provide insights into the mechanisms underlying DNA binding. Copyright (c) 2013 International Union of Crystallography urn:issn:1744-3091 Chen, S.-C. Huang, C.-H. Chen, Y.-R. Yang, C.S. Lin, C.-T. Chen, Y. 2013-05-25 doi:10.1107/S1744309113012943 International Union of Crystallography The DNA-binding domain of the response regulator SaeR was crystallized. Determination of its structure will reveal the residues that are critical for protein–DNA recognition. EN two-component systems SaeR Staphylococcus epidermidis SaeR is the response regulator of the SaeRS two-component signal transduction system, which is involved in regulating bacterial autolysis and biofilm formation. SaeR comprises an N-terminal receiver domain and a C-terminal effector domain. The effector domain possesses DNA-binding and transactivation functions. Here, the effector domain of SaeR from Staphylococcus epidermidis was purified and crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 2.15 Å and belonged to space group P212121, with unit-cell parameters a = 34.20, b = 53.78, c = 111.66 Å. Determining the structure will provide insights into the mechanisms underlying DNA binding. text/html Crystallization and preliminary X-ray diffraction analysis of the DNA-binding domain of the response regulator SaeR from Staphylococcus epidermidis text 6 69 2013-05-25 Copyright (c) 2013 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 0 0