issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

June 2010 issue

Highlighted illustration

Cover illustration: 1.4 Å resolution structure of Paracoccus pantotrophus pseudoazurin (Najmudin et al., p. 627).

structural communications


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The crystal structure of the photosynthetic A4 isoform of glyceraldehyde-3-phosphate dehydrogenase from the model plant A. thaliana has been solved at 2.6 Å resolution. The tetrameric structure includes four molecules of NAD and eight sulfate ions occupying the P sites involved in catalysis.

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A high-resolution structure of P. pantrotrophus pseudoazurin is reported at 1.4 Å resolution, together with secondary-structure-based sequence alignment of the type 1 copper protein family.

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The crystal structure of FeoA from Stenotrophomonas maltophilia has been determined to a resolution of 1.7 Å using an Se single-wavelength anomalous dispersion (Se-SAD) approach and revealed a unique dimer cross-linked by two zinc ions and six chloride ions.

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The crystal structure of the phosphatase domain of Sts-1 at pH 4.6 complexed with sulfate has been determined to 1.35 Å resolution.

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The crystal structure of PhaZ7 depolymerase determined at atomic (1.2 Å) resolution in the presence of PMSF reveals a preformed serine protease catalytic triad and details of the architecture of the active site.

crystallization communications



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Soluble N-terminal domain of yeast magnesium ion transporter Mrs2 was overexpressed in E. coli, purified, crystallized and X-ray diffraction data collected to 1.83 Å resolution.

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A DNA-binding protein from S. virginiae was crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to approximately 3.0 Å resolution.

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Deuterated type III antifreeze protein specifically hydrogen reverse-labelled in the methyl groups of leucine and valine residues has been expressed, purified and crystallized. Preliminary neutron data collection showed diffraction to 1.80 Å resolution from a 0.23 mm3 crystal.

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The catalytic module of endolysin from the phage Cp-7 was crystallized using the vapour-diffusion method. Native data were collected to 2.4 Å resolution.

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The C-terminal domain of mouse hepatitis virus nucleocapsid protein has been overexpressed in E. coli, purified and crystallized. The crystal belonged to space group P422, with unit-cell parameters a = 66.6, c = 50.8 Å, and diffracted to 2.20 Å resolution.

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L-Rhamnose isomerase (L-RhI) from B. halodurans has been purified and crystallized. The crystals of L-RhI belonged to the monoclinic space group P21, with unit-cell parameters a = 83.2, b = 164.9, c = 92.0 Å, β = 116.0°, and diffracted to 2.5 Å resolution.

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Different forms of the magnesium-ion transporter CorC have been crystallized; crystallization was affected by nucleotides and magnesium ions.

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The transporters of the bacterial phosphotransferase system mediate the uptake of carbohydrates with concomitant phosphorylation. Good-quality crystals have been obtained of the membrane-spanning EIICGlc domain of the E. coli glucose transporter.


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The glycosylated fungal haem-thiolate peroxygenase AaPII was crystallized in three different forms from a charge-heterogeneous protein sample. Structure solution of the 45 kDa protein was achieved with SAD utilizing the haem iron and the structure was determined at 2.2 Å resolution.

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PrTX-I, a noncatalytic and myotoxic Lys49-phospholipase A2 from B. pirajai venom, was cocrystallized with the inhibitor rosmarinic acid from C. verbenacea. The crystals diffracted X-rays to 1.8 Å resolution and the structure was solved, indicating a remarkable electronic density for the ligand at the entrance to the hydrophobic channel.

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Crystallization of glycosylated human prolylcarboxypeptidase expressed in Chinese hamster ovary cells is described. The hexagonal crystals belong to space group R32 and diffract to 2.8 Å resolution.

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The gene segment encoding avian infectious bronchitis virus nonstructural protein 9 has been cloned and expressed in Escherichia coli. The protein has been crystallized and the crystals diffracted X-rays to 2.44 Å resolution.

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Ethanolamine ammonia-lyase from E. coli has been overexpressed, purified and crystallized. The crystals diffracted to 2.2 Å resolution using synchrotron radiation.

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The ferredoxin reductase component of carbazole 1,9a-dioxygenase (Red) is involved in electron transfer from NAD(P)H to ferredoxin. The class IIA Red from Novosphingobium sp. KA1 was crystallized and the crystal diffracted to a resolution of 1.58 Å.

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Thermostable recombinant L2 lipase from thermophilic Bacillus sp. L2 has been crystallized by using counter-diffusion method and diffracted to 2.7 Å resolution. The crystal belongs to the primitive orthorhombic space group P212121 with unit-cell parameters a = 87.44, b = 94.90, c = 126.46 Å.

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SeMet-substituted pyridoxal 4-dehydrogenase from M. loti MAFF303099 was crystallized and diffraction data were collected to 2.9 Å resolution.


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GIMAP2, a guanine nucleotide-binding protein belonging to the GIMAP family, has been crystallized in various nucleotide-loaded states.

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Crystals of the complex between the Fab fragment of a human anti-EphA2 antibody and the N-terminal domain of human EphA2 have been obtained. Diffraction data were collected to 2.55 Å resolution.

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Crystals of the R2 subunit from the oncovirus Kaposi's sarcoma-associated γ-herpesvirus (KSHV) were obtained by the use of in situ proteolysis. The crystals diffracted to 2.0 Å resolution and belonged to space group P21.

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The enzyme 3-isopropylmalate dehydrogenase (IPMDH) from T. thermophilus, which catalyses the penultimate reaction step of the leucine-biosynthesis pathway, has been crystallized in various states along its reaction coordinate.

laboratory communications


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New types of aggregation suppressors, such as amino acids and their derivatives, were focused on as fourth-component additives. Data were obtained that indicated that the additives promote protein crystallization.

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During the past two decades, amino acids and amino-acid derivatives have been applied in various fields of protein chemistry. The potential use of amino acids and their derivatives as new precipitating agents is described.
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