issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

December 2007 issue

Highlighted illustration

Cover illustration: Allophycocyanin from Thermosynechococcus elongatus [Murray et al. (2007), Acta Cryst. F63, 998-1002].

structural genomics communications


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The crystal structure of the minimized α/β-hydrolase fold protein encoded by the gene TTHA1544 from T. thermophilus HB8 has been determined at 2.0 Å resolution.

protein structure communications


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The crystal structure of a light-harvesting protein that interacts with photosystem II is reported.

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The crystal structure of MnSOD with four dimers per asymmetric unit was refined to an R factor of 21.1% at 1.8 Å resolution. Differences in the monomer fold and dimer interface relative to the human enzyme can be exploited in the design of selective drugs for Bacillus MnSOD.

nucleic acid structure communications


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The structure of the complex of the hexanucleotide duplex d(CGCGCA)·d(TGCGCG) with hexammineruthenium(III) ion shows a tautomeric shift in the adenine base and a consequent disruption of the A·T base pair.

crystallization communications


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A vertebrate-type [2Fe–2S] ferredoxin (FdxB), which is probably involved in the iron–sulfur cluster-biosynthesis system of the γ-proteobacterium P. putida JCM 20004, has been crystallized in space group P6122. The needle-shaped crystals of recombinant FdxB diffract to 1.90 Å resolution using synchrotron radiation.

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I-Dmo-I is a well characterized homing endonuclease from the archaeon Desulfurococcus mobilis. The enzyme was cloned and overexpressed in Escherichia coli. Crystallization experiments of I-Dmo-I in complex with its DNA target in the presence of Ca2+ and Mg2+ yielded crystals that were suitable for X-ray diffraction analysis.

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The production and crystallization of human leukocyte antigen class II molecules HLA-DQ2 and HLA-DQ8 in complex with deamidated gliadin peptides is reported. Crystals of HLA-DQ2PQPELPYPQ diffracted to 3.9 Å, while the HLA-DQ8EGSFQPSQE crystals diffracted to 2.1 Å, allowing structure determination by molecular replacement.

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The C-terminal catalytic domain of serine/threonine kinase RSK1 has been crystallized; the crystals diffracted to a resolution of 2.7 Å and belonged to space group P21.

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Mutation of symmetry-related (in space group P43212) glutamate and lysine residues on the water-exposed surface of an integral membrane protein, cytochrome ba3, from T. thermophilus leads to robust crystallization of the protein in space group P41212; crystals of these mutant proteins show X-ray diffraction to molecular resolution.


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HA3, a 70 kDa haemagglutinating protein, is a precursor form of HA3a and HA3b, the subcomponents of Clostridium botulinum type C 16S progenitor toxin. In this report, recombinant HA3 protein was overexpressed in Escherichia coli, purified and crystallized.

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In this study, the Korean pine (Pinus koraiensis) vicilin-type 7S seed storage protein was isolated from defatted pine-nut extract and purified by sequential gel-filtration and anion-exchange chromatography. Well diffracting single crystals were obtained by the vapour-diffusion method in hanging drops.

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The cloning, expression, purification and crystallization of the CBM3b module of cellobiohydrolase 9A from C. thermocellum is described. The crystals diffract to 2.68 Å.

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A putative member of the haloacid dehalogenase superfamily from T. onnurineus has been expressed, purified and crystallized using 1.6 M magnesium sulfate as a precipitant. The crystals belonged to the triclinic space group P1 and diffracted to 1.8 Å resolution.

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The crystallization of ybfF, a new esterase from E. coli, and the collection of diffraction data to 1.1 Å resolution are reported.

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The expression, purification and crystallization of human 5-lipoxygenase-activating protein in complex with two leukotriene-biosynthesis inhibitors is decribed. The processes that were used to generate diffraction quality crystals are presented in detail.

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ScpB from M. tuberculosis was crystallized using the sitting-drop vapour-diffusion method in the presence of 2 M NaCl and 10% PEG 6000 at 295 K. X-­ray diffraction data were collected to a maximum resolution of 2.3 Å at a synchrotron beamline.

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The antiproliferative complex Tob–hCaf1 was purified and crystallized using the sitting-drop vapour-diffusion method. The crystal diffracted to around 2.6 Å resolution.

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Crystals scattering to 2.00 Å resolution have been obtained of the ydjA nitroreductase from E. coli K12.

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Crotoxin B is a basic phospholipase A2 found in the venom of C. durissus terrificus and is one of the subunits that constitute crotoxin. Here, the crystallization, X-ray diffraction data collection and molecular-replacement solution of a novel tetrameric complex formed by two dimers of crotoxin B isoforms are presented.

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Crystals of the plant Rho protein ROP5 from A. thaliana have been obtained that diffract to 1.53 Å resolution.

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Crystals of baculovirus-expressed adeno-associated virus serotype 7 capsids have been produced which diffract X-rays to ∼3.0 Å resolution.

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The expression, purification and crystallization of the small laccase from S. coelicolor are reported. Diffraction data were collected to 3 Å resolution.

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Three data sets have been collected on endothiapepsin complexed with the gem-diol inhibitor PD-135,040: a high-resolution synchrotron X-ray data set, a room-temperature X-ray data set and a neutron diffraction data set. Until recently, it has been impossible to grow large protein crystals of endothiapepsin with any gem-diol inhibitor that are suitable for neutron diffraction.

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Nucleoside diphosphate kinase from B. anthracis has been crystallized. Preliminary crystallographic analysis shows that there is one monomer in the asymmetric unit of the crystal.

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A ternary complex of the proteinase inhibitor (BTCI) with trypsin and chymotrypsin was crystallized and its crystal structure was solved by molecular replacement.
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