http://journals.iucr.org/f/issues/2010/02/00/isscontsbdy.html Acta Crystallographica Section F Structural Biology and Crystallization Communications aims to provide a home for communications on the crystallization and structure determination of biological macromolecules. It will commence publication in January 2005 and will include three categories of publication: Structural genomics communications, Protein structure communications, Crystallization communications. Articles will be available online when ready, making publication as fast as possible, and will include unlimited free colour illustrations, movies and other enhancements. The editorial process will be completely electronic with respect to deposition, submission, refereeing and publication. en Copyright (c) 2010 International Union of Crystallography 2010-02-01 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 aims to provide a home for communications on the crystallization and structure determination of biological macromolecules. It will commence publication in January 2005 and will include three categories of publication: Structural genomics communications, Protein structure communications, Crystallization communications. Articles will be available online when ready, making publication as fast as possible, and will include unlimited free colour illustrations, movies and other enhancements. The editorial process will be completely electronic with respect to deposition, submission, refereeing and publication. text/html Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Volume 66, Part 2, 2010 text monthly 1 2002-01-01T00:00+00:00 2 66 2010-02-01 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications 112 urn:issn:1744-3091 med@iucr.org February 2010 2010-02-01 http://journals.iucr.org/logos/rss10f.gif http://journals.iucr.org/f/issues/2010/02/00/isscontsbdy.html Still image http://scripts.iucr.org/cgi-bin/paper?me0416 Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Baker, E.N. Dauter, Z. Einspahr, H. Weiss, M.S. 2010-01-28 doi:10.1107/S1744309110001326 International Union of Crystallography en Editorial text/html In defence of our science – validation now! text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications editorial 112 112 http://scripts.iucr.org/cgi-bin/paper?kw5017 Bovine pancreatic ribonuclease A (RNase A) was crystallized from a mixture of small molecules containing basic fuchsin, tobramycin and uridine 5′-monophosphate (U5P). Solution of the crystal structure revealed that the enzyme was selectively bound to U5P, with the pyrimidine ring of U5P residing in the pyrimidine-binding site at Thr45. The structure was refined to an R factor of 0.197 and an Rfree of 0.253. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Larson, S.B. Day, J.S. Nguyen, C. Cudney, R. McPherson, A. 2010-01-26 doi:10.1107/S174430910905194X International Union of Crystallography The crystal structure of bovine pancreatic ribonuclease A in complex with uridine 5′-monophosphate was determined at 1.60 Å resolution. The uridine lies in the pyrimidine-specific binding site of the enzyme, with the phosphate group extended into the solvent without interacting with the protein. en ribonuclease A uridine 5′-monophosphate silver bullets Bovine pancreatic ribonuclease A (RNase A) was crystallized from a mixture of small molecules containing basic fuchsin, tobramycin and uridine 5′-monophosphate (U5P). Solution of the crystal structure revealed that the enzyme was selectively bound to U5P, with the pyrimidine ring of U5P residing in the pyrimidine-binding site at Thr45. The structure was refined to an R factor of 0.197 and an Rfree of 0.253. text/html Structure of bovine pancreatic ribonuclease complexed with uridine 5′-monophosphate at 1.60 Å resolution text 2 66 2010-01-26 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 113 120 http://scripts.iucr.org/cgi-bin/paper?hv5137 The crystal structure of Bacillus amyloliquefaciens α-amylase (BAA) at 1.4 Å resolution revealed ambiguities in the thermal adaptation of homologous proteins in this family. The final model of BAA is composed of two molecules in a back-to-back orientation, which is likely to be a consequence of crystal packing. Despite a high degree of identity, comparison of the structure of BAA with those of other liquefying-type α-amylases indicated moderate discrepancies at the secondary-structural level. Moreover, a domain-displacement survey using anisotropic B-factor and domain-motion analyses implied a significant contribution of domain B to the total flexibility of BAA, while visual inspection of the structure superimposed with that of B. licheniformis α-amylase (BLA) indicated higher flexibility of the latter in the central domain A. Therefore, it is suggested that domain B may play an important role in liquefying α-amylases, as its rigidity offers a substantial improvement in thermostability in BLA compared with BAA. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Alikhajeh, J. Khajeh, K. Ranjbar, B. Naderi-Manesh, H. Lin, Y.-H. Liu, E. Guan, H.-H. Hsieh, Y.-C. Chuankhayan, P. Huang, Y.-C. Jeyaraman, J. Liu, M.-Y. Chen, C.-J. 2010-01-26 doi:10.1107/S1744309109051938 International Union of Crystallography The crystal structure of B. amyloliquefaciens α-amylase (BAA) at 1.4 Å resolution revealed ambiguities in the thermal adaptation of homologous proteins in this family. en α-amylases thermostability flexibility alignment The crystal structure of Bacillus amyloliquefaciens α-amylase (BAA) at 1.4 Å resolution revealed ambiguities in the thermal adaptation of homologous proteins in this family. The final model of BAA is composed of two molecules in a back-to-back orientation, which is likely to be a consequence of crystal packing. Despite a high degree of identity, comparison of the structure of BAA with those of other liquefying-type α-amylases indicated moderate discrepancies at the secondary-structural level. Moreover, a domain-displacement survey using anisotropic B-factor and domain-motion analyses implied a significant contribution of domain B to the total flexibility of BAA, while visual inspection of the structure superimposed with that of B. licheniformis α-amylase (BLA) indicated higher flexibility of the latter in the central domain A. Therefore, it is suggested that domain B may play an important role in liquefying α-amylases, as its rigidity offers a substantial improvement in thermostability in BLA compared with BAA. text/html Structure of Bacillus amyloliquefaciens α-amylase at high resolution: implications for thermal stability text 2 66 2010-01-26 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 121 129 http://scripts.iucr.org/cgi-bin/paper?tb5012 The crystal structure of Vibrio cholerae uracil-DNA N-glycosylase (vcUNG) has been determined to 1.5 Å resolution. Based on this structure, a homology model of Aliivibrio salmonicida uracil-DNA N-glycosylase (asUNG) was built. A previous study demonstrated that asUNG possesses typical cold-adapted features compared with vcUNG, such as a higher catalytic efficiency owing to increased substrate affinity. Specific amino-acid substitutions in asUNG were suggested to be responsible for the increased substrate affinity and the elevated catalytic efficiency by increasing the positive surface charge in the DNA-binding region. The temperature adaptation of these enzymes has been investigated using structural and mutational analyses, in which mutations of vcUNG demonstrated an increased substrate affinity that more resembled that of asUNG. Visualization of surface potentials revealed a more positive potential for asUNG compared with vcUNG; a modelled double mutant of vcUNG had a potential around the substrate-binding region that was more like that of asUNG, thus rationalizing the results obtained from the kinetic studies. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Raeder, I.L.U. Moe, E. Willassen, N.P. Smalås, A.O. Leiros, I. 2010-01-26 doi:10.1107/S1744309109052063 International Union of Crystallography The crystal structure of uracil-DNA N-glycosylase from Vibrio cholerae has been determined at 1.5 Å, and used for mapping temperature adaptation. en cold adaptation mutational analysis uracil-DNA N-glycosylase Aliivibrio salmonicida Vibrio cholerae The crystal structure of Vibrio cholerae uracil-DNA N-glycosylase (vcUNG) has been determined to 1.5 Å resolution. Based on this structure, a homology model of Aliivibrio salmonicida uracil-DNA N-glycosylase (asUNG) was built. A previous study demonstrated that asUNG possesses typical cold-adapted features compared with vcUNG, such as a higher catalytic efficiency owing to increased substrate affinity. Specific amino-acid substitutions in asUNG were suggested to be responsible for the increased substrate affinity and the elevated catalytic efficiency by increasing the positive surface charge in the DNA-binding region. The temperature adaptation of these enzymes has been investigated using structural and mutational analyses, in which mutations of vcUNG demonstrated an increased substrate affinity that more resembled that of asUNG. Visualization of surface potentials revealed a more positive potential for asUNG compared with vcUNG; a modelled double mutant of vcUNG had a potential around the substrate-binding region that was more like that of asUNG, thus rationalizing the results obtained from the kinetic studies. text/html Structure of uracil-DNA N-glycosylase (UNG) from Vibrio cholerae: mapping temperature adaptation through structural and mutational analysis text 2 66 2010-01-26 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 130 136 http://scripts.iucr.org/cgi-bin/paper?sw5034 Copper amine oxidases (CAOs) are ubiquitous in nature and catalyse the oxidative deamination of primary amines to the corresponding aldehydes. Humans have three viable CAO genes (AOC1–3). AOC1 encodes human diamine oxidase (hDAO), which is the frontline enzyme for histamine metabolism. hDAO is unique among CAOs in that it has a distinct substrate preference for diamines. The structure of hDAO in space group P212121 with two molecules in the asymmetric unit has recently been reported. Here, the structure of hDAO refined to 2.1 Å resolution in space group C2221 with one molecule in the asymmetric unit is reported. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 McGrath, A.P. Hilmer, K.M. Collyer, C.A. Dooley, D.M. Guss, J.M. 2010-01-27 doi:10.1107/S1744309109052130 International Union of Crystallography The structure of human diamine oxidase has been refined to 2.1 Å resolution in space group C2221. en diamine oxidases copper amine oxidases topaquinone histaminase kidney amine oxidases Copper amine oxidases (CAOs) are ubiquitous in nature and catalyse the oxidative deamination of primary amines to the corresponding aldehydes. Humans have three viable CAO genes (AOC1–3). AOC1 encodes human diamine oxidase (hDAO), which is the frontline enzyme for histamine metabolism. hDAO is unique among CAOs in that it has a distinct substrate preference for diamines. The structure of hDAO in space group P212121 with two molecules in the asymmetric unit has recently been reported. Here, the structure of hDAO refined to 2.1 Å resolution in space group C2221 with one molecule in the asymmetric unit is reported. text/html A new crystal form of human diamine oxidase text 2 66 2010-01-27 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 137 142 http://scripts.iucr.org/cgi-bin/paper?fw5244 The AMP-activated protein kinase (AMPK) is a highly conserved trimeric protein complex that is responsible for energy homeostasis in eukaryotic cells. Here, a 1.9 Å resolution crystal structure of the isolated kinase domain from the α2 subunit of human AMPK, the first from a multicellular organism, is presented. This human form adopts a catalytically inactive state with distorted ATP-binding and substrate-binding sites. The ATP site is affected by changes in the base of the activation loop, which has moved into an inhibited DFG-out conformation. The substrate-binding site is disturbed by changes within the AMPKα2 catalytic loop that further distort the enzyme from a catalytically active form. Similar structural rearrangements have been observed in a yeast AMPK homologue in response to the binding of its auto-inhibitory domain; restructuring of the kinase catalytic loop is therefore a conserved feature of the AMPK protein family and is likely to represent an inhibitory mechanism that is utilized during function. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Littler, D.R. Walker, J.R. Davis, T. Wybenga-Groot, L.E. Finerty, P.J. Newman, E. Mackenzie, F. Dhe-Paganon, S. 2010-01-27 doi:10.1107/S1744309109052543 International Union of Crystallography A 1.9 Å resolution crystal structure of the isolated kinase domain from the α2 subunit of human AMPK, the first from a multicellular organism, is presented. en AMP-activated kinases kinases DFG-out conformation The AMP-activated protein kinase (AMPK) is a highly conserved trimeric protein complex that is responsible for energy homeostasis in eukaryotic cells. Here, a 1.9 Å resolution crystal structure of the isolated kinase domain from the α2 subunit of human AMPK, the first from a multicellular organism, is presented. This human form adopts a catalytically inactive state with distorted ATP-binding and substrate-binding sites. The ATP site is affected by changes in the base of the activation loop, which has moved into an inhibited DFG-out conformation. The substrate-binding site is disturbed by changes within the AMPKα2 catalytic loop that further distort the enzyme from a catalytically active form. Similar structural rearrangements have been observed in a yeast AMPK homologue in response to the binding of its auto-inhibitory domain; restructuring of the kinase catalytic loop is therefore a conserved feature of the AMPK protein family and is likely to represent an inhibitory mechanism that is utilized during function. text/html A conserved mechanism of autoinhibition for the AMPK kinase domain: ATP-binding site and catalytic loop refolding as a means of regulation text 2 66 2010-01-27 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 143 151 http://scripts.iucr.org/cgi-bin/paper?en5397 The 1.6 Å resolution structure of the micromolar competitive inhibitor S-(N,N-dimethylaminoethyl) phenylacetothiohydroximate-O-sulfate bound to Sinapis alba myrosinase, a plant thioglucosidase, is reported. Myrosinase and its substrates, the glucosinolates, are part of the plant's defence system. The sulfate group and the phenyl group of the inhibitor bind to the aglycon-binding site of the enzyme, whereas the N,N-dimethyl group binds to the glucose-binding site and explains the large improvement in binding affinity compared with previous compounds. The structure suggests ways to increase the potency and specificity of the compound by improving the interactions with the hydrophobic pocket of the aglycon-binding site. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Besle, A. Brazzolotto, X. Tatibouët, A. Cerniauskaite, D. Gallienne, E. Rollin, P. Burmeister, W.P. 2010-01-27 doi:10.1107/S1744309109052865 International Union of Crystallography The crystal structure of an O-sulfated thiohydroximate inhibitor bound to S. alba myrosinase is reported. en thioglucosidases myrosinase family 1 glycosyl hydrolases glucosinolates inhibitors The 1.6 Å resolution structure of the micromolar competitive inhibitor S-(N,N-dimethylaminoethyl) phenylacetothiohydroximate-O-sulfate bound to Sinapis alba myrosinase, a plant thioglucosidase, is reported. Myrosinase and its substrates, the glucosinolates, are part of the plant's defence system. The sulfate group and the phenyl group of the inhibitor bind to the aglycon-binding site of the enzyme, whereas the N,N-dimethyl group binds to the glucose-binding site and explains the large improvement in binding affinity compared with previous compounds. The structure suggests ways to increase the potency and specificity of the compound by improving the interactions with the hydrophobic pocket of the aglycon-binding site. text/html A micromolar O-sulfated thiohydroximate inhibitor bound to plant myrosinase text 2 66 2010-01-27 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications structural communications 152 155 http://scripts.iucr.org/cgi-bin/paper?xb5002 RspB is a surface adhesin of Erysipelothrix rhusiopathiae. A recombinant form of the collagen-binding region of this protein, RspB(31–348), has been overexpressed in Escherichia coli in native and selenomethionine-derivative forms and purified using affinity and gel-permeation chromatography. Thin plate-like crystals were obtained by the hanging-drop vapour-diffusion method using the same condition for both forms. The native crystals diffracted to a resolution of 2.5 Å using an in-house X-ray source, while the selenomethionine-derivative crystals diffracted to a resolution of 2.2 Å using synchrotron radiation. The crystals belonged to the monoclinic space group P21, with unit-cell parameters a = 46.19, b = 66.65, c = 101.72 Å, β = 94.11°. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Devi, A.S. Ogawa, Y. Shimoji, Y. Ponnuraj, K. 2010-01-27 doi:10.1107/S1744309109035581 International Union of Crystallography The expression, purification and crystallization of the collagen-binding region of the E. rhusiopathiae surface protein RspB is described. The crystals diffracted to 2.2 Å resolution using synchrotron radiation. en RspB Erysipelothrix rhusiopathiae collagen binding RspB is a surface adhesin of Erysipelothrix rhusiopathiae. A recombinant form of the collagen-binding region of this protein, RspB(31–348), has been overexpressed in Escherichia coli in native and selenomethionine-derivative forms and purified using affinity and gel-permeation chromatography. Thin plate-like crystals were obtained by the hanging-drop vapour-diffusion method using the same condition for both forms. The native crystals diffracted to a resolution of 2.5 Å using an in-house X-ray source, while the selenomethionine-derivative crystals diffracted to a resolution of 2.2 Å using synchrotron radiation. The crystals belonged to the monoclinic space group P21, with unit-cell parameters a = 46.19, b = 66.65, c = 101.72 Å, β = 94.11°. text/html Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the collagen-binding region of RspB from Erysipelothrix rhusiopathiae text 2 66 2010-01-27 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 156 159 http://scripts.iucr.org/cgi-bin/paper?hc5089 d,d-Heptose-1,7-bisphosphate phosphatase (GmhB), which is involved in the third step of the NDP-heptose biosynthesis pathway, converts d,d-heptose-1,7-bisphosphate to d,d-heptose-1-phosphate. This biosynthesis pathway is a target for new antibiotics or antibiotic adjuvants for Gram-negative pathogens. Burkholderia thailandensis is a useful surrogate organism for studying the pathogenicity of melioidosis owing to its extensive genomic similarity to B. pseudomallei. Melioidosis caused by B. pseudomallei is a serious invasive disease of animals and humans in tropical and subtropical areas. In this study, GmhB has been cloned, expressed, purified and crystallized. X-ray data have also been collected to 2.50 Å resolution using synchrotron radiation. The crystal belonged to space group P6, with unit-cell parameters a = 243.2, b = 243.2, c = 41.1 Å. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Kim, M.-S. Shin, D.H. 2010-01-27 doi:10.1107/S1744309109042614 International Union of Crystallography In this study, d,d-heptose-1,7-bisphosphate phosphatase has been cloned, expressed, purified and crystallized. en d,d-heptose-1,7-bisphosphate phosphatase Burkholderia thailandensis NDP-heptose biosynthesis d,d-Heptose-1,7-bisphosphate phosphatase (GmhB), which is involved in the third step of the NDP-heptose biosynthesis pathway, converts d,d-heptose-1,7-bisphosphate to d,d-heptose-1-phosphate. This biosynthesis pathway is a target for new antibiotics or antibiotic adjuvants for Gram-negative pathogens. Burkholderia thailandensis is a useful surrogate organism for studying the pathogenicity of melioidosis owing to its extensive genomic similarity to B. pseudomallei. Melioidosis caused by B. pseudomallei is a serious invasive disease of animals and humans in tropical and subtropical areas. In this study, GmhB has been cloned, expressed, purified and crystallized. X-ray data have also been collected to 2.50 Å resolution using synchrotron radiation. The crystal belonged to space group P6, with unit-cell parameters a = 243.2, b = 243.2, c = 41.1 Å. text/html A preliminary X-ray study of d,d-heptose-1,7-bisphosphate phosphatase from Burkholderia thailandensis E264 text 2 66 2010-01-27 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 160 162 http://scripts.iucr.org/cgi-bin/paper?bw5320 The opium poppy Papaver somniferum is the source of the narcotic analgesics morphine and codeine. Salutaridine reductase (SalR; EC 1.1.1.248) reduces the C-7 keto group of salutaridine to the C-7 (S)-hydroxyl group of salutaridinol in the biosynthetic pathway that leads to morphine in the opium poppy plant. P. somniferum SalR was overproduced in Escherichia coli and purified using cobalt-affinity and size-exclusion chromatography. Hexagonal crystals belonging to space group P6422 or P6222 were obtained using ammonium sulfate as precipitant and diffracted to a resolution of 1.9 Å. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Higashi, Y. Smith, T.J. Jez, J.M. Kutchan, T.M. 2010-01-27 doi:10.1107/S174430910904932X International Union of Crystallography Recombinant P. somniferum salutaridine reductase (SalR) was purified and crystallized with NADPH using the hanging-drop vapor-diffusion method. Crystals of the SalR–NADPH complex diffracted X-rays to a resolution of 1.9 Å. en Papaver somniferum salutaridine reductase SDR family plant secondary metabolism The opium poppy Papaver somniferum is the source of the narcotic analgesics morphine and codeine. Salutaridine reductase (SalR; EC 1.1.1.248) reduces the C-7 keto group of salutaridine to the C-7 (S)-hydroxyl group of salutaridinol in the biosynthetic pathway that leads to morphine in the opium poppy plant. P. somniferum SalR was overproduced in Escherichia coli and purified using cobalt-affinity and size-exclusion chromatography. Hexagonal crystals belonging to space group P6422 or P6222 were obtained using ammonium sulfate as precipitant and diffracted to a resolution of 1.9 Å. text/html Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferum text 2 66 2010-01-27 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 163 166 http://scripts.iucr.org/cgi-bin/paper?bw5325 The antitoxin Phd from the phd/doc module of bacteriophage P1 was crystallized in two distinct crystal forms. Crystals of His-tagged Phd contain a C-terminally truncated version of the protein and diffract to 2.20 Å resolution. Crystals of untagged Phd purified from the Phd–Doc complex diffract to 2.25 Å resolution. These crystals are partially merohedrally twinned and contain the full-length version of the protein. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Garcia-Pino, A. Sterckx, Y. Vandenbussche, G. Loris, R. 2010-01-27 doi:10.1107/S1744309109051550 International Union of Crystallography The antitoxin Phd from the phd/doc operon of bacteriophage P1 was crystallized in two distinct crystal forms. en toxin–antitoxin ribosome intrinsic disorder transcription factors The antitoxin Phd from the phd/doc module of bacteriophage P1 was crystallized in two distinct crystal forms. Crystals of His-tagged Phd contain a C-terminally truncated version of the protein and diffract to 2.20 Å resolution. Crystals of untagged Phd purified from the Phd–Doc complex diffract to 2.25 Å resolution. These crystals are partially merohedrally twinned and contain the full-length version of the protein. text/html Purification and crystallization of Phd, the antitoxin of the phd/doc operon text 2 66 2010-01-27 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 167 171 http://scripts.iucr.org/cgi-bin/paper?en5400 Human hookworms are among the most pathogenic soil-transmitted helminths. These parasitic nematodes have co-evolved with the host and are able to maintain a high worm burden for decades without killing the human host. However, it is possible to develop vaccines against laboratory-challenge hookworm infections using either irradiated third-state infective larvae (L3) or enzymes from the adult parasites. In an effort to control hookworm infection globally, the Human Hookworm Vaccine Initiative, a product-development partnership with the Sabin Vaccine Institute to develop new control tools including vaccines, has identified a battery of protein antigens, including surface-associated antigens (SAAs) from L3. SAA proteins are characterized by a 13 kDa conserved domain of unknown function. SAA proteins are found on the surface of infective L3 stages (and some adult stages) of different nematode parasites, suggesting that they may play important roles in these organisms. The atomic structures and function of SAA proteins remain undetermined and in an effort to remedy this situation recombinant Na-SAA-2 from the most prevalent human hookworm parasite Necator americanus has been expressed, purified and crystallized. Useful X-ray data have been collected to 2.3 Å resolution from a crystal that belonged to the monoclinic space group C2 with unit-cell parameters a = 73.88, b = 35.58, c = 42.75 Å, β = 116.1°. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Asojo, O.A. Goud, G.N. Zhan, B. Ordonez, K. Sedlacek, M. Homma, K. Deumic, V. Gupta, R. Brelsford, J. Price, M.K. Ngamelue, M.N. Hotez, P.J. 2010-01-27 doi:10.1107/S1744309109051616 International Union of Crystallography The purification, crystallization and preliminary X-ray diffraction analysis of a surface-associated antigen from the major human hookworm N. americanus is presented. en surface-associated antigens hookworm Necator americanus ancylostoma vaccines Human hookworms are among the most pathogenic soil-transmitted helminths. These parasitic nematodes have co-evolved with the host and are able to maintain a high worm burden for decades without killing the human host. However, it is possible to develop vaccines against laboratory-challenge hookworm infections using either irradiated third-state infective larvae (L3) or enzymes from the adult parasites. In an effort to control hookworm infection globally, the Human Hookworm Vaccine Initiative, a product-development partnership with the Sabin Vaccine Institute to develop new control tools including vaccines, has identified a battery of protein antigens, including surface-associated antigens (SAAs) from L3. SAA proteins are characterized by a 13 kDa conserved domain of unknown function. SAA proteins are found on the surface of infective L3 stages (and some adult stages) of different nematode parasites, suggesting that they may play important roles in these organisms. The atomic structures and function of SAA proteins remain undetermined and in an effort to remedy this situation recombinant Na-SAA-2 from the most prevalent human hookworm parasite Necator americanus has been expressed, purified and crystallized. Useful X-ray data have been collected to 2.3 Å resolution from a crystal that belonged to the monoclinic space group C2 with unit-cell parameters a = 73.88, b = 35.58, c = 42.75 Å, β = 116.1°. text/html Crystallization and preliminary X-ray analysis of Na-SAA-2 from the human hookworm parasite Necator americanus text 2 66 2010-01-27 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 172 176 http://scripts.iucr.org/cgi-bin/paper?ub5004 The minor pilin FctB is an integral part of the pilus assembly expressed by Streptococcus pyogenes. Since it is located at the cell wall, it can be hypothesized that it functions as a cell-wall anchor for the streptococcal pilus. In order to elucidate its structure, the genes for FctB from the S. pyogenes strains 90/306S and SF370 were cloned for overexpression in Escherichia coli. FctB from strain 90/306S was crystallized by the sitting-drop vapour-diffusion method using sodium citrate as a precipitant. The hexagonal FctB crystals belonged to space group P61 or P65, with unit-cell parameters a = b = 95.15, c = 100.25 Å, and diffracted to 2.9 Å resolution. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Linke, C. Young, P.G. Kang, H.J. Proft, T. Baker, E.N. 2010-01-28 doi:10.1107/S1744309109051951 International Union of Crystallography The minor pilin FctB from S. pyogenes strain 90/306S was expressed in E. coli, purified and crystallized. The hexagonal FctB crystals diffracted to 2.9 Å resolution. en bacterial pili polymer assembly Streptococcus pyogenes FctB minor pilins The minor pilin FctB is an integral part of the pilus assembly expressed by Streptococcus pyogenes. Since it is located at the cell wall, it can be hypothesized that it functions as a cell-wall anchor for the streptococcal pilus. In order to elucidate its structure, the genes for FctB from the S. pyogenes strains 90/306S and SF370 were cloned for overexpression in Escherichia coli. FctB from strain 90/306S was crystallized by the sitting-drop vapour-diffusion method using sodium citrate as a precipitant. The hexagonal FctB crystals belonged to space group P61 or P65, with unit-cell parameters a = b = 95.15, c = 100.25 Å, and diffracted to 2.9 Å resolution. text/html Purification, crystallization and preliminary crystallographic analysis of the minor pilin FctB from Streptococcus pyogenes text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 177 179 http://scripts.iucr.org/cgi-bin/paper?pu5282 The study of proteins involved in de novo biosynthesis of purine nucleotides is central in the development of antibiotics and anticancer drugs. In view of this, a protein from the hyperthermophile Pyrococcus horikoshii OT3 was isolated, purified and crystallized using the microbatch method. Its primary structure was found to be similar to that of SAICAR synthetase, which catalyses the seventh step of de novo purine biosynthesis. A diffraction-quality crystal was obtained using Hampton Research Crystal Screen II condition No. 34, consisting of 0.05 M cadmium sulfate hydrate, 0.1 M HEPES buffer pH 7.5 and 1.0 M sodium acetate trihydrate, with 40%(v/v) 1,4-butanediol as an additive. The crystal belonged to space group P31, with unit-cell parameters a = b = 95.62, c = 149.13 Å. Assuming the presence of a hexamer in the asymmetric unit resulted in a Matthews coefficient (VM) of 2.3 Å3 Da−1, corresponding to a solvent content of about 46%. A detailed study of this protein will yield insights into structural stability at high temperatures and should be highly relevant to the development of antibiotics and anticancer drugs targeting the biosynthesis of purine nucleotides. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Manjunath, K. Jeyakanthan, J. Nakagawa, N. Shinkai, A. Yoshimura, M. Kuramitsu, S. Yokoyama, S. Sekar, K. 2010-01-28 doi:10.1107/S1744309109052026 International Union of Crystallography SAICAR synthetase from P. horikoshii OT3 has been cloned, expressed, purified and crystallized. en SAICAR synthetase PH0239 Pyrococcus horikoshii OT3 purine biosynthesis The study of proteins involved in de novo biosynthesis of purine nucleotides is central in the development of antibiotics and anticancer drugs. In view of this, a protein from the hyperthermophile Pyrococcus horikoshii OT3 was isolated, purified and crystallized using the microbatch method. Its primary structure was found to be similar to that of SAICAR synthetase, which catalyses the seventh step of de novo purine biosynthesis. A diffraction-quality crystal was obtained using Hampton Research Crystal Screen II condition No. 34, consisting of 0.05 M cadmium sulfate hydrate, 0.1 M HEPES buffer pH 7.5 and 1.0 M sodium acetate trihydrate, with 40%(v/v) 1,4-butanediol as an additive. The crystal belonged to space group P31, with unit-cell parameters a = b = 95.62, c = 149.13 Å. Assuming the presence of a hexamer in the asymmetric unit resulted in a Matthews coefficient (VM) of 2.3 Å3 Da−1, corresponding to a solvent content of about 46%. A detailed study of this protein will yield insights into structural stability at high temperatures and should be highly relevant to the development of antibiotics and anticancer drugs targeting the biosynthesis of purine nucleotides. text/html Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of the putative SAICAR synthetase (PH0239) from Pyrococcus horikoshii OT3 text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 180 183 http://scripts.iucr.org/cgi-bin/paper?nj5048 1,3-Propanediol dehydrogenase is an enzyme that catalyzes the oxidation of 1,3-propanediol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. SeMet-labelled 1,3-propanediol dehydrogenase protein from the hyperthermophilic bacterium Aquifex aeolicus VF5 was overexpressed in Escherichia coli and purified to homogeneity. Crystals of this protein were grown from an acidic buffer with ammonium sulfate as the precipitant. Single-wavelength data were collected at the selenium peak to a resolution of 2.4 Å. The crystal belonged to space group P32, with unit-cell parameters a = b = 142.19, c = 123.34 Å. The structure contained two dimers in the asymmetric unit and was solved by the MR-SAD approach. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Jeyakanthan, J. Thamotharan, S. Panjikar, S. Kitamura, Y. Nakagawa, N. Shinkai, A. Kuramitsu, S. Yokoyama, S. 2010-01-28 doi:10.1107/S1744309109052403 International Union of Crystallography 1,3-Propanediol dehydrogenase (Aq_1145) from A. aeolicus VF5 has been overexpressed, purified and crystallized. The crystals diffracted to 2.4 Å resolution. en 1,3-propanediol dehydrogenase Aquifex aeolicus VF5 Aq_1145 1,3-Propanediol dehydrogenase is an enzyme that catalyzes the oxidation of 1,3-propanediol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. SeMet-labelled 1,3-propanediol dehydrogenase protein from the hyperthermophilic bacterium Aquifex aeolicus VF5 was overexpressed in Escherichia coli and purified to homogeneity. Crystals of this protein were grown from an acidic buffer with ammonium sulfate as the precipitant. Single-wavelength data were collected at the selenium peak to a resolution of 2.4 Å. The crystal belonged to space group P32, with unit-cell parameters a = b = 142.19, c = 123.34 Å. The structure contained two dimers in the asymmetric unit and was solved by the MR-SAD approach. text/html Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) from Aquifex aeolicus VF5 text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 184 186 http://scripts.iucr.org/cgi-bin/paper?bo5072 Glycine decarboxylase, or P-protein, is a major enzyme that is involved in the C1 metabolism of all organisms and in the photorespiratory pathway of plants and cyanobacteria. The protein from Synechocystis sp. PCC 6803 is a homodimer with a mass of 215 kDa. Recombinant glycine decarboxylase was expressed in Escherichia coli and purified by metal-affinity, ion-exchange and gel-filtration chromatography. Crystals of P-protein that diffracted to a resolution of 2.1 Å were obtained using the hanging-drop vapour-diffusion method at 291 K. X-ray diffraction data were collected from cryocooled crystals using synchrotron radiation. The crystals belonged to space group P212121, with unit-cell parameters a = 96.30, b = 135.81, c = 179.08 Å. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Hasse, D. Hagemann, M. Andersson, I. Bauwe, H. 2010-01-28 doi:10.1107/S1744309109052828 International Union of Crystallography Recombinant glycine decarboxylase from Synechocystis sp. PCC 6803 was expressed in E. coli and purified to homogeneity. Crystals were obtained that diffracted to 2.1 Å resolution using synchrotron radiation. en glycine decarboxylases P-proteins Glycine decarboxylase, or P-protein, is a major enzyme that is involved in the C1 metabolism of all organisms and in the photorespiratory pathway of plants and cyanobacteria. The protein from Synechocystis sp. PCC 6803 is a homodimer with a mass of 215 kDa. Recombinant glycine decarboxylase was expressed in Escherichia coli and purified by metal-affinity, ion-exchange and gel-filtration chromatography. Crystals of P-protein that diffracted to a resolution of 2.1 Å were obtained using the hanging-drop vapour-diffusion method at 291 K. X-ray diffraction data were collected from cryocooled crystals using synchrotron radiation. The crystals belonged to space group P212121, with unit-cell parameters a = 96.30, b = 135.81, c = 179.08 Å. text/html Crystallization and preliminary X-ray diffraction analyses of the homodimeric glycine decarboxylase (P-protein) from the cyanobacterium Synechocystis sp. PCC 6803 text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 187 191 http://scripts.iucr.org/cgi-bin/paper?hc5096 The DEAD-box RNA helicase DDX5 is involved in many aspects of RNA processing and has been implicated in a number of cellular processes involving alteration of RNA secondary structure. The N-terminal region of DDX5, which contains the conserved domain 1 of the DEAD-box helicases, has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of this region is reported. X-ray diffraction data were processed to a resolution of 2.7 Å. The crystals belonged to space group I222, with unit-cell parameters a = 66.18, b = 73.80, c = 104.00 Å, α = β = γ = 90°. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Choi, Y.-W. Dutta, S. Fielding, B.C. Tan, Y.-J. 2010-01-28 doi:10.1107/S1744309109052956 International Union of Crystallography The production and crystallization of the human DEAD box polypeptide 5 are reported. A 2.7 Å native diffraction data set has been obtained. en DEAD-box helicases DDX5 The DEAD-box RNA helicase DDX5 is involved in many aspects of RNA processing and has been implicated in a number of cellular processes involving alteration of RNA secondary structure. The N-terminal region of DDX5, which contains the conserved domain 1 of the DEAD-box helicases, has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of this region is reported. X-ray diffraction data were processed to a resolution of 2.7 Å. The crystals belonged to space group I222, with unit-cell parameters a = 66.18, b = 73.80, c = 104.00 Å, α = β = γ = 90°. text/html Expression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5 text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 192 194 http://scripts.iucr.org/cgi-bin/paper?bo5069 Growth factor receptor-bound protein 2 (Grb2) is an adaptor protein with a single SH2 domain that specifically binds to focal adhesion kinase (FAK) when residue Tyr925 of FAK is phosphorylated. The Grb2–FAK interaction is associated with cellular integrin-activated signal transduction events leading to the activation of the Ras-MAPK pathway. Crystals of the Grb2 SH2 domain in complex with a phosphopeptide corresponding to residues 921–930 of FAK have been obtained using the sitting-drop vapour-diffusion technique. The crystals belonged to space group P3121, with unit-cell parameters a = b = 102.7, c = 127.6 Å, α = β = 90.0, γ = 120.0°. A diffraction data set was collected from a flash-cooled crystal at 100 K to 2.49 Å resolution using synchrotron radiation. Structure determination by molecular replacement and analysis of the detailed structure of the complex are currently in progress. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Chen, H.-H. Chen, C.-W. Chang, Y.-Y. Shen, T.-L. Hsu, C.-H. 2010-01-28 doi:10.1107/S1744309109053184 International Union of Crystallography Crystals of the Grb2 SH2 domain in complex with a phosphotyrosyl peptide corresponding to residues 921–930 of focal adhesion kinase (FAK) have been obtained using the sitting-drop vapour-diffusion technique. Data have been collected to 2.49 Å resolution. en Grb2 SH2 domain FAK Growth factor receptor-bound protein 2 (Grb2) is an adaptor protein with a single SH2 domain that specifically binds to focal adhesion kinase (FAK) when residue Tyr925 of FAK is phosphorylated. The Grb2–FAK interaction is associated with cellular integrin-activated signal transduction events leading to the activation of the Ras-MAPK pathway. Crystals of the Grb2 SH2 domain in complex with a phosphopeptide corresponding to residues 921–930 of FAK have been obtained using the sitting-drop vapour-diffusion technique. The crystals belonged to space group P3121, with unit-cell parameters a = b = 102.7, c = 127.6 Å, α = β = 90.0, γ = 120.0°. A diffraction data set was collected from a flash-cooled crystal at 100 K to 2.49 Å resolution using synchrotron radiation. Structure determination by molecular replacement and analysis of the detailed structure of the complex are currently in progress. text/html Preliminary crystallographic characterization of the Grb2 SH2 domain in complex with a FAK-derived phosphotyrosyl peptide text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 195 197 http://scripts.iucr.org/cgi-bin/paper?uo5003 The Toll signalling pathway, which is crucial for innate immunity, is transduced in insect haemolymph via a proteolytic cascade consisting of three serine proteases. The proteolytic cascade is downregulated by a specific serine protease inhibitor (serpin). Recently, the serpin SPN48 was found to show an unusual specific reactivity towards the terminal serine protease, Spätzle-processing enzyme, in the beetle Tenebrio molitor. In this study, the mature form of SPN48 was overexpressed in Escherichia coli and purified. The purified SPN48 protein was crystallized using 14% polyethylene glycol 8000 and 0.1 M 2-(N-morpholino)ethanesulfonic acid pH 6.0 as the precipitant. The crystals diffracted X-rays to 2.1 Å resolution and were suitable for structure determination. The crystals belonged to space group P21. The crystal structure will provide information regarding how SPN48 achieves its unusual specificity for its target protease. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Park, S.H. Piao, S. Kwon, H.-M. Kim, E.-H. Lee, B.L. Ha, N.-C. 2010-01-28 doi:10.1107/S1744309109053147 International Union of Crystallography In this study, the mature form of SPN48 was overexpressed in Escherichia coli and purified. The purified SPN48 protein was crystallized using 14% polyethylene glycol 8000 and 0.1 M 2-(N-morpholino)ethanesulfonic acid pH 6.0 as the precipitant. The crystals diffracted X-rays to 2.1 Å resolution and were suitable for structure determination. en serpins Tenebrio molitor SPN48 The Toll signalling pathway, which is crucial for innate immunity, is transduced in insect haemolymph via a proteolytic cascade consisting of three serine proteases. The proteolytic cascade is downregulated by a specific serine protease inhibitor (serpin). Recently, the serpin SPN48 was found to show an unusual specific reactivity towards the terminal serine protease, Spätzle-processing enzyme, in the beetle Tenebrio molitor. In this study, the mature form of SPN48 was overexpressed in Escherichia coli and purified. The purified SPN48 protein was crystallized using 14% polyethylene glycol 8000 and 0.1 M 2-(N-morpholino)ethanesulfonic acid pH 6.0 as the precipitant. The crystals diffracted X-rays to 2.1 Å resolution and were suitable for structure determination. The crystals belonged to space group P21. The crystal structure will provide information regarding how SPN48 achieves its unusual specificity for its target protease. text/html Crystallization and preliminary X-ray crystallographic analysis of a highly specific serpin from the beetle Tenebrio molitor text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 198 200 http://scripts.iucr.org/cgi-bin/paper?bw5324 VSP1 is a defence protein in Arabidopsis thaliana that may also be involved in control of plant development. The recombinant protein has been overexpressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method. The crystal diffracted to 1.9 Å resolution and a complete X-ray data set was collected at 100 K using Cu Kα radiation from a rotating-anode X-ray source. The crystals belonged to space group C2. As there are no related structures that could be used as a search model for molecular replacement, work is in progress on experimental phasing using heavy-atom derivatives and selenomethionine derivatives. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Shi, Z.-B. Ge, H.-H. Zhao, P. Zhang, M. 2010-01-28 doi:10.1107/S1744309109053688 International Union of Crystallography VSP1 from Arabidopsis thaliana was expressed in E. coli, purified and crystallized. X-ray diffraction data were collected to 1.9 Å resolution. en VSP1 Arabidopsis thaliana defence proteins VSP1 is a defence protein in Arabidopsis thaliana that may also be involved in control of plant development. The recombinant protein has been overexpressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method. The crystal diffracted to 1.9 Å resolution and a complete X-ray data set was collected at 100 K using Cu Kα radiation from a rotating-anode X-ray source. The crystals belonged to space group C2. As there are no related structures that could be used as a search model for molecular replacement, work is in progress on experimental phasing using heavy-atom derivatives and selenomethionine derivatives. text/html Crystallization and preliminary crystallographic analysis of recombinant VSP1 from Arabidopsis thaliana text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 201 203 http://scripts.iucr.org/cgi-bin/paper?ll5211 Psu, a coat protein from bacteriophage P4, inhibits Rho-dependent transcription termination both in vivo and in vitro. The Psu protein is α-helical in nature and appeared to be a dimer in solution. It interacts with Rho and affects the ATP binding and RNA-dependent ATPase activity of Rho, which in turn reduces the rate of RNA release from the elongation complex. Crystals of Psu were grown in space group I422 in the presence of PEG, with unit-cell parameters a = b = 148.76, c = 63.38 Å and a calculated Matthews coefficient of 2.1 Å3 Da−1 (41.5% solvent content), assuming the presence of two molecules in the asymmetric unit. A native data set was collected to 2.3 Å resolution. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Khamrui, S. Ranjan, A. Pani, B. Sen, R. Sen, U. 2010-01-28 doi:10.1107/S1744309109053846 International Union of Crystallography Psu, a unique 21 kDa protein from bacteriophage P4, is a non-essential capsid-decoration protein that inhibits Rho-dependent termination specifically and efficiently both in vivo and in vitro. Psu has been crystallized using PEG as precipitant and the crystals diffracted to 2.3 Å resolution. en Rho Psu transcription termination Psu, a coat protein from bacteriophage P4, inhibits Rho-dependent transcription termination both in vivo and in vitro. The Psu protein is α-helical in nature and appeared to be a dimer in solution. It interacts with Rho and affects the ATP binding and RNA-dependent ATPase activity of Rho, which in turn reduces the rate of RNA release from the elongation complex. Crystals of Psu were grown in space group I422 in the presence of PEG, with unit-cell parameters a = b = 148.76, c = 63.38 Å and a calculated Matthews coefficient of 2.1 Å3 Da−1 (41.5% solvent content), assuming the presence of two molecules in the asymmetric unit. A native data set was collected to 2.3 Å resolution. text/html Crystallization and preliminary X-ray analysis of Psu, an inhibitor of the bacterial transcription terminator Rho text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 204 206 http://scripts.iucr.org/cgi-bin/paper?hc5093 Transcription elongation by eukaryotic RNA polymerase II requires the coupling of mRNA synthesis and mRNA processing and export. The essential protein Iws1 is at the interface of these processes through its interaction with histone chaperone and elongation factor Spt6 as well as with complexes involved in mRNA processing and export. Upon crystallization of the evolutionarily conserved domain of Iws1 from Encephalitozoon cuniculi, four different crystal forms were obtained. Three of the crystal forms belonged to space group P21 and one belonged to space group P2221. Preliminary X-ray crystallographic analysis of one of the crystal forms allowed the collection of data to 2.5 Å resolution. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Koch, M. Diebold, M.-L. Cavarelli, J. Romier, C. 2010-01-28 doi:10.1107/S1744309109052749 International Union of Crystallography E. cuniculi Iws1, which acts in eukaryotic transcription and mRNA processing and export, has been crystallized and data have been collected to 2.5 Å resolution. en Iws1 Encephalitozoon cuniculi eukaryotic transcription factors mRNA export factors Transcription elongation by eukaryotic RNA polymerase II requires the coupling of mRNA synthesis and mRNA processing and export. The essential protein Iws1 is at the interface of these processes through its interaction with histone chaperone and elongation factor Spt6 as well as with complexes involved in mRNA processing and export. Upon crystallization of the evolutionarily conserved domain of Iws1 from Encephalitozoon cuniculi, four different crystal forms were obtained. Three of the crystal forms belonged to space group P21 and one belonged to space group P2221. Preliminary X-ray crystallographic analysis of one of the crystal forms allowed the collection of data to 2.5 Å resolution. text/html Crystallization and preliminary crystallographic analysis of eukaryotic transcription and mRNA export factor Iws1 from Encephalitozoon cuniculi text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 207 210 http://scripts.iucr.org/cgi-bin/paper?en5405 Fas-associated factor 1 (FAF1) is a multifunctional pro-apoptotic protein that is involved in Fas-mediated apoptosis, NF-κB signalling and the ubiquitin–proteasome pathway. In the ubiquitin–proteasome pathway, FAF1 binds to the N domain of p97/VCP, a molecular chaperone that acts in complex with the proteasome, through its C-terminal UBX domain and inhibits the proteasomal protein-degradation process. In an effort to elucidate the structural basis of the function of FAF1 in modulating p97/VCP activity related to proteasomal protein degradation, crystallographic analysis of the FAF1 UBX domain and the p97/VCP N domain was initiated. Following the recently reported crystallization of the FAF1 UBX domain bound to the p97/VCP N domain, the unbound FAF1 UBX domain was also crystallized for purposes of structural comparison. X-ray data were collected to 3.00 Å resolution and the crystals belonged to space group F4132, with unit-cell parameters a = b = c = 176.40 Å. The Matthews coefficient and solvent content were estimated to be 3.04 Å3 Da−1 and 59.5%, respectively, assuming that the asymmetric unit contained two molecules of the UBX domain, which was subsequently confirmed by molecular-replacement calculations. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Kang, W. Shin, H.Y. Yang, J.K. 2010-01-28 doi:10.1107/S1744309110001077 International Union of Crystallography The FAF1 UBX domain was crystallized. X-ray diffraction data were collected to 3.00 Å resolution and the crystals belonged to space group F4132. en Fas-associated factor 1 FAF1 UBX domain Fas-associated factor 1 (FAF1) is a multifunctional pro-apoptotic protein that is involved in Fas-mediated apoptosis, NF-κB signalling and the ubiquitin–proteasome pathway. In the ubiquitin–proteasome pathway, FAF1 binds to the N domain of p97/VCP, a molecular chaperone that acts in complex with the proteasome, through its C-terminal UBX domain and inhibits the proteasomal protein-degradation process. In an effort to elucidate the structural basis of the function of FAF1 in modulating p97/VCP activity related to proteasomal protein degradation, crystallographic analysis of the FAF1 UBX domain and the p97/VCP N domain was initiated. Following the recently reported crystallization of the FAF1 UBX domain bound to the p97/VCP N domain, the unbound FAF1 UBX domain was also crystallized for purposes of structural comparison. X-ray data were collected to 3.00 Å resolution and the crystals belonged to space group F4132, with unit-cell parameters a = b = c = 176.40 Å. The Matthews coefficient and solvent content were estimated to be 3.04 Å3 Da−1 and 59.5%, respectively, assuming that the asymmetric unit contained two molecules of the UBX domain, which was subsequently confirmed by molecular-replacement calculations. text/html Crystallization and preliminary X-ray crystallographic analysis of human FAF1 UBX domain text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications crystallization communications 211 213 http://scripts.iucr.org/cgi-bin/paper?hc9072 Additional funding is acknowledged by the authors of Hee et al. [Acta Cryst. (2009), F65, 422–425]. Copyright (c) 2010 International Union of Crystallography urn:issn:1744-3091 Hee, C.S. Gao, S. Miller, M.M. Goto, R.M. Ziegler, A. Daumke, O. Uchanska-Ziegler, B. 2010-01-28 doi:10.1107/S1744309110001089 International Union of Crystallography Addendum to Hee et al. [Acta Cryst. (2009), F65, 422–425]. en YF1*7.1 chicken Rfp-Y MHC class I antigens addendum Additional funding is acknowledged by the authors of Hee et al. [Acta Cryst. (2009), F65, 422–425]. text/html Expression, purification and preliminary X-ray crystallographic analysis of the chicken MHC class I molecule YF1*7.1. Addendum text 2 66 2010-01-28 Copyright (c) 2010 International Union of Crystallography Acta Crystallographica Section F: Structural Biology and Crystallization Communications addenda and errata 214 214