issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

April 2007 issue

Highlighted illustration

Cover illustration: Complex structure of a bacterial class 2 histone deacetylase homologue with a trifluoromethylketone inhibitor [Nielsen, Hildmann, Riester, Wegener, Schwienhorst & Ficner (2007), Acta Cryst. F63, 270-273].

protein structure communications


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Crystal structure analysis of the apo form of catabolite control protein A reveals the three-helix bundle of the DNA-binding domain. In the crystal packing, this domain interacts with the binding site for the corepressor protein.

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The crystal structure of a signalling glycoprotein isolated from buffalo dry secretions (SPB-40) has been determined at 2.8 Å resolution. Two unique residues, Tyr120 and Glu269, found in SPB-40 distort the shape of the sugar-binding groove considerably. The water structure in the groove is also different. The conformations of three flexible loops, His188–His197, Phe202–Arg212 and Tyr244–Pro260, also differ from those found in other structurally similar proteins.

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The crystal structure of a secreted chymotrypsin from the alkalophile Cellulomonas bogoriensis has been determined using data to 1.78 Å resolution.

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The crystal structure of HDAH FB188 in complex with a trifluoromethylketone at 2.2 Å resolution is reported and compared to a previously determined inhibitor complex.

structural genomics communications


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The structure of P. polycephalum cytochrome b5 reductase, an enzyme which catalyzes the reduction of cytochrome b5 by NADH, was determined at a resolution of 1.56 Å.

crystallization communications


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Glutaredoxin 2 from E. coli was cocrystallized with glutathione and data were collected to 1.60 Å. A mutant with the active-site residues Cys9 and Cys12 changed to serine was crystallized in the absence of glutathione and data were collected to 2.4 Å.

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Crystals of DDX3 RNA helicase domain have been obtained in a monoclinic form that diffract to 2.2 Å resolution using synchrotron radiation at the ID14-1 ESRF beamline.

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Crotoxin, a potent neurotoxin from the venom of the South American rattlesnake Crotalus durissus terrificus, exists as a heterodimer formed between a phospholipase A2 and a catalytically inactive acidic phospholipase A2 analogue (crotapotin). Large single crystals of the crotoxin complex and of the isolated subunits have been obtained.

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The crystallization and crystallographic data analysis of filamin repeats 14–16 are reported.

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A haloalkane dehalogenase, DbjA, was crystallized by the hanging-drop vapour-diffusion method using PEG 4000 as a precipitant. The crystal belongs to the orthorhombic system, space group P21212 and diffracts to 1.75 Å resolution.

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A leucine-zipper with properties as apoptotic regulator in the ER has been crystallized. X-ray data to 2.5 Å resolution were collected, molecular replacement solutions were identified and refinement has been started.

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The enzyme p-coumaric acid decarboxylase (PDC) from L. plantarum has been recombinantly expressed, purified and crystallized. The structure has been solved at 2.04 Å resolution by the molecular-replacement method.

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The genes encoding XMT and DXMT, the enzymes from Coffea canephora (robusta) that catalyse the three independent N-methyl transfer reactions in the caffeine-biosynthesis pathway, have been cloned and the proteins have been expressed in Escherichia coli. Both proteins have been crystallized in the presence of the demethylated cofactor S-adenosyl-L-cysteine (SAH) and substrate (xanthosine for XMT and theobromine for DXMT).

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The pyrimidine nucleoside phosphorylase TTHA1771 from T. thermophilus HB8 has been overexpressed, purified and crystallized. The crystals diffract X-rays to 1.8 Å resolution using synchrotron radiation.

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The reduced form of BphA3, a Rieske-type [2Fe–2S] ferredoxin, was crystallized by the sitting-drop vapour-diffusion method under anaerobic conditions. A molecular-replacement calculation yielded a satisfactory solution.

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To investigate the structural characteristics of a covalent inhibitor bound to porcine pancreatic elastase (PPE), including H atoms and hydration by water, a crystal of porcine pancreatic elastase with its inhibitor was grown to a size of 1.6 mm3 for neutron diffraction study. The crystal diffracted to 2.3 Å resolution with sufficient quality for further structure determination owing to the similar atomic scattering properties of deuterium and carbon.

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A Kunitz-type trypsin inhibitor purified from the seeds of Murraya koenigii has been crystallized by the sitting-drop vapour-diffusion method using PEG 8000 as the precipitating agent.

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Crystals of the human immunodeficiency virus 1 subtype C protease complexed with indinavir and nelfinavir have been grown in the monoclinic space group P21 and shown to diffract X-rays to 2.3 Å resolution.

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The molybdopterin synthase from T. thermophilus HB8 was cloned, expressed, purified and crystallized. The crystals belong to space group P21 and diffracted to a resolution of 1.64 Å.


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Isolated modules of mouse coactivator-associated arginine methyltransferase 1 encompassing the protein arginine N-methyltransferase catalytic domain have been overexpressed, purified and crystallized. X-ray diffraction data have been collected and have enabled determination of the structures by multiple isomorphous replacement using anomalous scattering.

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A truncated form of biotin carboxyl carrier protein containing the C-terminal half fragment (BCCPΔN76) and the biotin protein ligase (BPL) with the mutation R48A (BPL*) or the double mutation R48A K111A (BPL**) were successfully cocrystallized in the presence of ATP and biotin. The BPL*–BCCPΔN76 and BPL**–BCCPΔN76 crystals belong to space group P21 and diffract X-rays to 2.7 and 2.0 Å resolution, respectively.

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Crystals of human mitochondrial tyrosyl-tRNA synthetase lacking the C-terminal S4-like domain diffract to 2.7 Å resolution and are suitable for structure determination.

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The cytochrome P450 enzyme CYP203A1 from Rhodopseudomonas palustris binds a wide range of highly substituted aromatic compounds and may play an important role in the astonishing metabolic diversity of this organism. Crystals of CYP203A1 that diffract to 2.0 Å resolution have been obtained.

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A dimeric inert form of the replication initiator RepE of the F plasmid was expressed, purified and crystallized in complex with the repE operator DNA. Diffraction data were collected to 3.14 Å resolution.

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T. maritima mannitol dehydrogenase has been crystallized in space group P212121 with a = 84.43, b = 120.61, c = 145.76 Å. The crystals diffracted to 3.3 Å resolution at the Canadian Light Source.

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The phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv was crystallized and diffraction data were collected to 2.8 Å resolution.

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A CcdB homologue from V. fischeri was overexpressed in E. coli and purified. The free protein was crystallized, as were its complexes with fragments of E. coli and V. fischeri gyrase and with the F-plasmid CcdA C-terminal domain.
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