issue contents

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047

March 1997 issue

Highlighted illustration

Cover illustration: View of interdomain interface of cell adhesion molecule VCAM-D1D2. The two hydrophobic patches (yellow from domain 1 and orange from domain 2) allow the domains to rock back and forth around the `pivot' residue Tyr89. The long C'E loop and FG loop seem to guide the movement. Courtesy of Jia-huai Wang.

research papers


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High-resolution crystal structure of purine nucleoside phosphorylase has formed the foundation for a successful inhibitor design. A product of this design process, BCX-34, is currently undergoing clinical trials for treating T-cell lymphoma and T-cell leukemia. Resolving the ambiguity about the flexible loop covering the active site was the major achievement out of this refinement to high resolution.

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The structure of the first enzyme:inhibitor covalent adduct of factor D with diisopropyl fluorophosphate to a resolution of 2.4 Å is described. Comparisons between the active sites of native factor D, the adduct of factor D with diisopropyl fluorophosphate and diisopropyl fluorophosphate-inhibited trypsin have provided fundamental insights which are currently being employed in drug design.

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The X-ray structure of the cyclo-decapeptide, gramicidin S, is reported. it forms a twisted β-sheet, with two Phe residues in the D conformation to allow the necessary tight turns. Gramicidin S acts on cellular membranes, interacting with the lipid components, and the crystal symmetry generates a left-handed double spiral of molecules forming channels which could span the membrane.

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The structure of the 154-amino-acid form of basic fibroblast growth factor, refined at 2.0 Å resolution, shows the same Kunitz-type fold as the N-terminus truncated 146-amino-acid form, and the eight-amino-acid extension does not seem to lower the flexibilty observed in the N-terminal residues of the truncated form. The structure included one phosphate ion and one molecule of mercaptoethanol.

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The X-ray crystal structure of human plasminogen kringle 4 at 1.68 Å and 277 K is presented. Most of the ten disordered residues form two patches on the surface of the protein. This localized disorder suggests that these residues may play a role in quaternary assembly and possibly part of an interface with other domains of proteins with kringle domains, such as plasminogen.

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A method is described that detects structural features (such as secondary structure elements) in electron-density maps.

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The crystal structure of a Fab fragment directed against an important epitope of gp41 is described. The antigen-binding region is a pronounced groove and possible interactions with the peptide antigen are discussed.

short communications


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Crystals of the class IIb asparaginyl-tRNA synthetase of Thermus thermophilus, expressed in Escherichia coli, has been crystallized from PEG 6000 solutions. hydrophobic patches (yellow from domain 1 and orange from domain 2) allow the domains to rock back and forth around the `pivot', residue Tyr89. The long C'E loop and FG loop seem to guide the movement. Courtesy of Jia-huai Wang.

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The cytochrome b562 from Erwinia chrysanthemi has been crystallized in a form suitable for high-resolution data collection. the structure solution of this enzyme will allow a comparison with that from E. coli and lead to a better undertstanding of the electron-transfer mechanism.

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Isomorphous crystals of calgranulin C, an S100-like calcium-binding protein from pig granulocytes, were obtained in two different conditions. Crystals were characterized and a native data set collected to 2.6 Å resolution.

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Real-space refinement, alternated with reciprocal-space refinement, leads to models of higher quality than when refined exclusively in reciprocal space, even when starting with a map based on typically poor isomorphous replacement phases.

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Crystals of the FimC-FimH chaperone-adhesin pre-assembly complex from E. coli have been obtained. Data to 3.0 Å have been collected from a crystal frozen to T = 100 K.

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Human GM2-activator protein, expressed in E. coli, has been crystallized yielding well ordered crystals for X-ray diffraction analysis. The crystal space group is P212121, a = 42.4, b = 39.8, c = 113.6 Å.

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This paper describes the purification, crystallization and preliminary X-ray crystallographic and electron-microscopic characterization of a bacterial DNA helicase.

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Two crystal forms of 3-carboxy-cis,cis-muconate lactonizing enzyme have been characterized. The study of both crystal forms is being pursued to determine the crystal structure of this enzyme.

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Calystegia sepium agglutinin has been crystallized in an orthorhombic system with a dimer of identical 16 kDa subunits in the assymetric unit. A native data set to 2.0 Å resolution has been measured on a synchrotron source.


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Crystals of human recombinant cyclooxygenase-2 in complex with a selective inhibitor have been grown and analyzed. Analysis of protein in solution correlates with the dimeric structure found in the crystal. inn

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Nitrogenase from Klebsiella pneumoniae has been crystallized in two forms, one diffracting to 3.0 Å and the other to 1.5 Å. The X-ray analysis and MR solution is described.

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The conditions for the crystallization of xylose isomerase from Thermotoga neapolitana and the initial X-ray analysis of the crystals are described.
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