Severe diffraction anisotropy, rotational pseudosymmetry and twinning complicate the refinement of a pentameric coiled-coil structure of NSP4 of rotavirus

被引：7

作者：

Chacko, Anita R. ^{[1
]}

Zwart, Peter H. ^{[2
]}

Read, Randy J. ^{[3
]}

Dodson, Eleanor J. ^{[4
]}

Rao, C. D. ^{[5
]}

Suguna, Kaza ^{[1
]}

机构：

[1] Indian Inst Sci, Mol Biophys Unit, Bangalore 560012, Karnataka, India

[2] Univ Calif Berkeley, Lawrence Berkeley Natl Lab, Berkeley, CA 94720 USA

[3] Univ Cambridge, Dept Haematol, Cambridge Inst Med Res, Cambridge CB2 2XY, England

[4] Univ York, Dept Chem, York Struct Biol Lab, York YO10 5YW, N Yorkshire, England

[5] Indian Inst Sci, Dept Microbiol & Cell Biol, Bangalore 560012, Karnataka, India

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2012年 / 68卷

关键词：

ENTEROTOXIGENIC PROTEIN NSP4; NONSTRUCTURAL GLYCOPROTEIN; INTRACELLULAR CALCIUM; MOLECULAR REPLACEMENT; CRYSTAL-STRUCTURE; PSEUDO-SYMMETRY; INTERACTS; MEMBRANE; SOFTWARE; DOMAIN;

D O I：

10.1107/S090744491203836X

中图分类号：

Q5 [生物化学];

学科分类号：

070307 [化学生物学];

摘要：

The crystal structure of the region spanning residues 95-146 of the rotavirus nonstructural protein NSP4 from the asymptomatic human strain ST3 was determined at a resolution of 2.5 angstrom. Severe diffraction anisotropy, rotational pseudo-symmetry and twinning complicated the refinement of this structure. A systematic explanation confirming the crystal pathologies and describing how the structure was successfully refined is given in this report.

引用

页码：1541 / 1548

页数：8

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