issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

July 2008 issue

Highlighted illustration

Cover illustration: A putative molybdenum-cofactor biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472) (Yoshida et al., p. 589).

protein structure communications


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The crystal structure of Ynk1, an NDPK from the yeast Saccharomyces cerevisiae, has been solved at 3.1 Å resolution.

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The structures of complexes of the copper-containing amine oxidase from A. globiformis with benzylhydrazine and tranylcypromine have been refined at 1.86 and 1.65 Å resolution, respectively.

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The crystal structure of Escherichia coli AcrR with space group P31, which is distinct from our previously reported P2221 space-group structure, has been determined. A comparison of these two structures reveals possible mechanisms of ligand binding and AcrR regulation.

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The crystal structure of a putative molybdenum-cofactor biosynthesis protein C (MoaC) from S. tokodaii (ST0472) was determined at 2.2 Å resolution.

crystallization communications



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The α-haloacid dehalogenase DehI from P. putida strain PP3 was cloned into a vector with an N-terminal His tag and expressed in E. coli Nova Blue strain. Purified protein was crystallized in a primitive monoclinic form and a complete native data set was collected and analysed.

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The GppNHp-bound Rab27a GTPase in complex with exophilin4/Slp2-a has been purified and crystallized. Preliminary crystallographic analyses have been performed at 1.8 Å resolution.

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The production and crystallization of the tetratricopeptide-repeat domain of human small glutamine-rich tetratricopeptide-repeat protein are reported. A 2.4 Å native diffraction data set has been obtained.

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Trigonal crystals of MJ0729 showing different degrees of merohedral twinning that may vary from perfect hemihedral twinning to perfect tetartohedral twinning were obtained upon slight variation of the pH.

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Crystals of arylmalonate decarboxylase from A. bronchisepticus were obtained which diffracted X-rays to a resolution of at least 3.0 Å.

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Attempts have been made to crystallize the ligand-binding domain of the human retinoid X receptor in complex with a variety of newly synthesized ligands. An inverse correlation was observed between the `crystallizability' and the structural dynamics of the various receptor–ligand complexes.

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Crystals of the LOV1 domains of phototropin 1 and 2 from A. thaliana were obtained which diffracted X-rays to a resolution of at least 2.1 Å.

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Class II release factor 3 (RF3) from the sulfate-reducing bacterium D. vulgaris Miyazaki F has been overexpressed, purified and crystallized in complex with GDP.

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Site-directed mutagenesis has been applied to improve the overexpression and purification of the icosahedral enzyme lumazine synthase from B. subtilis as well as to produce a new crystal form. The mutant protein crystallizes in space group R3 and diffracts X-rays to 1.6 Å resolution.

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The genetically encoded fluorescent calcium-indicator protein GCaMP2 was crystallized in the calcium-saturated form. X-ray diffraction data were collected to 2.0 Å resolution and the structure was solved by molecular replacement.

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The ferredoxin component of carbazole 1,9a-dioxygenase (CARDO-F) is involved in an electron-transfer reaction. The CARDO-F from Novosphingobium sp. KA1 was crystallized under anaerobic conditions and diffracted to a resolution of 1.9 Å.

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Native and selenomethionine-derivative Abn2 have been expressed, purified and crystallized. Solution of the selenium substructure allowed the calculation of an initial experimental map at 2.7 Å resolution.

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Recombinant NUDT16 from human was expressed, purified and crystallized. The native crystals diffracted to 2.1 Å.


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The acidic polygalacturonase PehA from A. vitis has been crystallized. A molecular-replacement solution indicated a right-handed parallel β-helix fold.

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Orthorhombic crystals of a PduO-type ATP:cob(I)alamin adenosyltransferase from B. cereus were obtained both as an apoenzyme and in the presence of Mg2+ and ATP.

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The human voltage-dependent anion channel was overproduced in bacteria and refolded with the help of detergents. Extensive screening of crystallization conditions resulted in the first crystals to be obtained of this voltage-dependent anion-channel type. The crystals diffracted to a resolution of 3.6 Å.

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Truncation by the removal of the C-terminal hydrophobic transmembrane anchor has enabled the overexpression of a soluble domain of S. aureus YmfM in Escherichia coli, which has then been purified and subsequently crystallized.

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Dihydrodipicolinate synthase (DHDPS), an enzyme of the lysine-biosynthetic pathway, is a promising target for antibiotic development against pathogenic bacteria. Here, the expression, purification, crystallization and preliminary diffraction analysis to 1.45 Å resolution of DHDPS from methicillin-resistant S. aureus is reported.

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Urease from pigeon pea was purified and crystallized and X-ray diffraction data were collected at 2.5 Å resolution.

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Mouse galectin-4 carbohydrate binding domain was overexpressed in E. coli and crystallized in the presence of lactose. The crystals belong to tetragonal space group P4212 and diffraction data were collected to 2.1 Å resolution.

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Allene oxide synthase, an atypical cytochrome P450 from Parthenium argentatum, was crystallized and diffraction data were collected to 2.4 Å resolution.

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Single crystals of recombinant S-adenosyl-L-homocysteine hydrolase from L. luteus in complex with adenosine diffract X-rays to 1.17 Å resolution at 100 K. The crystals are tetragonal, space group P43212, and contain one copy of the dimeric enzyme in the asymmetric unit.
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