issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

April 2006 issue

Highlighted illustration

Cover illustration: The structure of SAICAR synthase monomer from T. maritima.

editorial


Acta Cryst. (2006). F62, 314
doi: 10.1107/S1744309106010347

protein structure communications


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The crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC 7942 in complex with NADP was determined at 2.5 Å resolution.

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The up-and-down binding of dimeric MecI to mecA dyad DNA may account for the cooperative effect of the repressor.

structural genomics communications


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The crystal structures of two crystal forms of manganese superoxide dismutase (Mn-SOD) from the radiation-resistant bacterium D. radiodurans are reported and compared with the crystal structure of Mn-SOD from E. coli.

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The crystal structure of human UBE2G2/UBC7 was solved at 2.56 Å resolution. The superimposition of UBE2G2 on UbcH7 in a c-Cbl–UbcH7–ZAP70 ternary complex suggested that the two loop regions of UBE2G2 interact with the RING domain in a similar way as UbcH7.

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The crystal structure of phophoribosylaminoimidazole-succinocarboxamide or SAICAR synthase from T. maritima at 2.2 Å revealed an unusual covalent dimer.

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The crystal structure of dimerized radixin FERM domain has been determined. It was found that the adhesion molecule-binding site of one molecule is masked by the C-terminal residues of the other molecule.

crystallization communications


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The heteromerization domain of an aminoacyl-tRNA synthetase cofactor from yeast was crystallized, complete selenomethionine MAD data were collected to 2.8 Å resolution and preliminary phasing reveals the presence of 20 monomers in the asymmetric unit.

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The crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from M. tuberculosis, are reported.

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The expression, purification and crystallization of a viral protease from the blotched snakehead virus (BSNV) are described and the diffraction data collected to 2.5 Å from two different crystal forms are reported.

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The M. tuberculosis prephenate dehydratase was cloned, expressed, purified, crystallized by the hanging-drop vapour-diffusion method, and a complete data set collected to 3.2 Å resolution using synchrotron radiation. These results should pave the way for the three-dimensional structure determination of the enzyme and provide a framework on which to base the rational design of chemotherapeutic agents to treat tuberculosis.

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The nucleocapsid protein of Bunyamwera virus, the prototypic member of the Bunyaviridae family of segmented negative-sense RNA viruses, has been expressed and crystallized. Complete X-ray diffraction data sets have been collected.

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The heme-containing membrane-associated fatty-acid α-dioxygenase pathogen-inducible oxygenase (PIOX) from O. sativa has been crystallized and a data set collected to 3.0 Å using a rotating-anode generator and R-AXIS IV detector.

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The RNA thiouridylase MnmA in complex with tRNA was crystallized with and without ATP in three different crystal forms, which may reflect distinct sulfuration-reaction stages.

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Crystals of the human Plk1 Polo-box domain in complex with a Cdc25C target peptide in an unphosphorylated and a phosphorylated state have been obtained in orthorhombic and monoclinic forms that diffract to 2.1 and 2.85 Å, respectively, using synchrotron radiation.

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SecDF is a multi-path membrane protein required for efficient protein translocation and integration via translocon. Purification and crystallization of T. thermophilus SecDF have been achieved by exploiting unique crystallization techniques that allowed the collection of a 3.74 Å data set.

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The AmyX gene encoding pullulanase from the common spore-forming bacterium B. subtilis strain 168 has been cloned, overexpressed in Escherichia coli, purified and crystallized.

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A low-molecular-weight cellulase from an alkalothermophilic Thermomonospora sp. has been crystallized. A diffraction data set has been collected to 2.3 Å resolution.

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Crystals of Anabaena sensory rhodopsin transducer, the transducer for the cyanobacterial photosensor Anabaena sensory rhodopsin, obtained in the space groups P4, C2 and P212121 diffract to 1.8, 2.1 and 2.0 Å, respectively. Phases for these crystal forms were obtained by SIRAS phasing using an iodide quick-soak derivative (P4) and molecular replacement (C2 and P212121).

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The human GTP fucose pyrophosphohydrolase protein has been crystallized via the hanging-drop technique over a reservoir of polyethylene glycol (MW 8000) and ethylene glycol. The orthorhombic crystals diffract to 2.8 Å resolution.

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Cytochrome P460 from N. europaea, a novel mono-heme protein containing an unusual lysine cross-link to the porphyrin ring, has been recombinantly expressed and purified from E. coli and crystallized. The crystals belong to the trigonal space group P31/221, with unit-cell parameters a = b = 53.3, c = 127.1 Å, one monomer in the asymmetric unit and diffract to 1.7 Å on a Cu Kα rotating-anode X-ray source.

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Deoxyuridine 5′-triphosphate nucleotidohydrolase from Mason–Pfizer monkey retrovirus (M-PMV dUTPase) is a betaretroviral member of the dUTPase enzyme family. The nucleocapsid-free dUTPase (48426 Da) was co-crystallized with a dUTP substrate analogue using the hanging-drop vapour-diffusion method.

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The C-terminal RNase III domain (RNase IIIb) of human Dicer has been expressed, purified and crystallized by the sitting-drop vapour-diffusion method.

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The SARS-CoV macro domain was expressed, purified and crystallized. Selenomethionine-labelled crystals diffracted to 1.8 Å resolution.

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Crystals of Nsp15 from the aetiological agent of SARS have been grown at room temperature. Crystals have cubic symmetry and diffract to a maximum resolution of 2.7 Å.

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RecA superfamily ATPase PH0284 from P. horikoshii OT3 was overexpressed, purified, crystallized and cocrystallized with ATP. Both crystal forms belong to the trigonal space group P3221 and diffract X-rays to 2.0 and 2.3 Å resolution, respectively.

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The outer membrane protein OmpW from E. coli was overexpressed in inclusion bodies and refolded with the help of detergent. The protein has been crystallized and the crystals diffract to 3.5 Å resolution.

addenda and errata


Acta Cryst. (2006). F62, 422
doi: 10.1107/S1744309106007391
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