issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

February 2012 issue

Highlighted illustration

Cover illustration: Structure of Helicobacter pylori neutrophil-activating protein (HP-NAP) (Tsuruta et al., pp. 134).

structural communications


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Crystal structures of human tankyrase I in complex with small-molecule inhibitors PJ34 and XAV939 have been determined, both to 2.0 Å. The TNKS1-PJ34 system allows for displacement soaking and, therefore, is an ideal system for structure-based drug design.

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The 0.85 Å room-temperature ultrahigh-resolution structure of H/D-exchanged crambin is reported. Preliminary 1.1 Å resolution neutron diffraction data have been collected at the neutron Protein Crystallography Station at LANSCE.

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The structures of new crystal forms of M. tuberculosis peptidyl-tRNA hydrolase confirm and provide further elaboration of the functionally relevant plasticity of the enzyme molecule.

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The first crystal structure of a pectin methylesterase from an enteropathogen is presented. This enzyme from Y. enterocolitica has biological significance for the evolution of pectin-metabolic pathways within pectinolytic bacteria and related agents of foodborne illness.

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A new crystal lattice structure of H. pylori neutrophil-activating protein has been determined. Iron loading causes a series of conformational changes at the ferroxidase centre.


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The interleukin-2 tyrosine kinase Src homology 2 domain was crystallized and its structure was solved to 2.35 Å resolution. The structure reveals a domain-swapped dimer that is related to other dimeric SH2 domains solved previously. The cistrans-prolyl isomerization that is evident from solution studies of Itk SH2 cannot be observed in the crystal structure.

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An unusual case of trace amounts of a contaminating protein facilitating formation of a heterotrimeric protein complex.

crystallization communications


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The N-terminal F-BAR domain of mouse PACSIN 3, which contains 341 amino acids, has been successfully cloned, purified and crystallized.

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A recombinant ATP-dependent DNA ligase from the hyperthermophilic anaerobic archaeon Thermococcus sibiricus was expressed in Escherichia coli and purified. Crystals were grown by vapour diffusion using the hanging-drop method.

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The C-terminal domain of the bacteriophage T7 fibre protein gp17, consisting of amino acids 371–553, has been crystallized. Diffraction data have been obtained to around 2.0 Å resolution from two different crystal forms. Multiwavelength anomalous dispersion phasing with a mercury derivative is in progress.

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Orthorhombic crystals of DtxR from T. acidophilum have been obtained. X-ray data were collected to 1.8 Å resolution using synchrotron radiation.

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The preliminary X-ray analysis of LipC12, the first lipase isolated through a metagenomics approach to be crystallized, is reported.

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The M. tuberculosis DNA gyrase A C-terminal domain (CTD) was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to space group P212121 and diffraction data were collected to a resolution of 1.55 Å.

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The expression, purification and crystallization of a soluble construct of the putative inner membrane protein PelD from P. aeruginosa is described. The crystals diffracted to a resolution of 2.2 Å.

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Several DNA and RNA fragments containing tandem AAAAAA repeats, which were synthesized as analogues of the A-rich repeats found in the autoregulatory sequence of PABP mRNA, have been crystallized, suggesting the possibility that the autoregulatory sequence has a specific structure which impedes the binding of PABP.

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Baculovirus envelope protein ODV-E66 (67–704) was crystallized; the crystal diffracted to 1.8 Å resolution and belonged to space group P62 or P64, with unit-cell parameters a = b = 113.5, c = 101.5 Å.

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Dioscorin from D. japonica was expressed, purified and crystallized using the sitting-drop vapour-diffusion method. The dioscorin crystal diffracted X-rays to 2.11 Å resolution.

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B. cereus arylamine N-acetyltransferase 3 was expressed, purified and crystallized. X-ray diffraction data were collected to 2.42 Å resolution and the crystals belonged to the monoclinic space group C121.

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S-Ribosylhomocysteinase (LuxS) encoded by the LuxS gene from Streptococcus mutans was solubly expressed in Escherichia coli, purified and crystallized. Diffraction by the crystal extended to 2.4 Å resolution.

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Native and selenomethionine-derivatized (SeMet) crystals of Bacillus subtilis YwfE in the presence of ADP, MgCl2 and the dipeptide L-Ala-L-Gln were obtained using the hanging-drop vapour-diffusion method.

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Aspartyl aminopeptidase (APP) is a metallopeptidase that catalyzes the hydrolysis of aspartic acid from the N-termini of polypeptide chains. The apeB gene from P. aeruginosa was cloned, the APP enzyme was expressed and crystallized and a preliminary X-ray crystallographic study was performed in order to understand its unique reaction pathway.

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An L-amino-acid oxidase from B. jararacussu venom was crystallized and X-ray diffraction data were collected to a maximum resolution of 3.0 Å.

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The expression, purification and crystallization of human dipeptidyl peptidase 10, a component of voltage-gated potassium channels, is described.

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The coiled-coil domain of the essential DNA-repair protein RecN from D. radiodurans was crystallized. The crystals belonged to space group P21 and diffracted X-rays to 2.04 Å resolution.

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Protein E of the respiratory pathogen H. influenzae is a multifunctional adhesin that is involved in bacterial attachment to host epithelium and direct interactions with vitronectin, laminin and plasminogen. The method of crystallization and X-ray data collection for protein E at 1.8 Å is presented.

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The nontoxic nonhaemagglutinin of serotype D neurotoxin complex, which is important in proteolytic stability for toxin complex, was expressed in E. coli, and crystallized.

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The refolding, purification and crystallization of FrpB from the meningitis pathogen Neisseria meningitidis is described.

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CPIP1 from N. tabacum (NtCPIP1) is a plant heat-shock 40-type protein that participates in effector–host interactions during potyviral infections. Whereas crystals of full-length wild-type NtCPIP1 only diffracted to 8.0 Å resolution, diffraction from crystals of a shortened variant lacking the first 127 amino acids extended to 2.4 Å resolution.

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A ribokinase gene (rbk) from the anaerobic halothermophilic bacterium Halothermothrix orenii was cloned and overexpressed in Escherichia coli. The recombinant protein (Ho-Rbk) was purified using immobilized metal-ion affinity chromatography and crystals were obtained using the sitting-drop method.

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Orotate phosphoribosyltransferase from Plasmodium falciparum produced in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method in complex with OA and PRPP in the presence of Mg2+.

international union of crystallography


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