Structure of pig heart citrate synthase at 1.78 Å resolution

被引：14

作者：

Larson, Steven B. ^{[1
]}

Day, John S. ^{[1
]}

Nguyen, Chieugiang ^{[2
]}

Cudney, Robert ^{[2
]}

McPherson, Alexander ^{[1
]}

机构：

[1] Univ Calif Irvine, Dept Mol Biol & Biochem, Irvine, CA 92697 USA

[2] Hampton Res, Aliso Viejo, CA 92656 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2009年 / 65卷

关键词：

REFINEMENT; STRATEGY; MODEL;

D O I：

10.1107/S1744309109008343

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Pig heart citrate synthase was crystallized from a small-molecule cocktail containing cystamine dihydrochloride, aspartame and benzamidine hydrochloride. The structure was refined to an R factor of 0.179 (R-free = 0.222) using synchrotron data to a resolution of 1.78 angstrom. The model includes the full-length protein, a chloride ion, a sulfate ion, 305 water molecules and an unexpected moiety attached through a disulfide linkage to Cys184, which was modeled as a half-cystamine molecule generated by disulfide exchange with the cystamine in the small-molecule cocktail.

引用

页码：430 / 434

页数：5

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