CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDIES OF GI-ALPHA-1 AND MUTANTS OF GI-ALPHA-1 IN THE GTP AND GDP-BOUND STATES

被引：46

作者：

COLEMAN, DE

LEE, E

MIXON, MB

LINDER, ME

BERGHUIS, AM

GILMAN, AG

SPRANG, SR

机构：

[1] UNIV TEXAS,SW MED CTR,HOWARD HUGHES MED INST,DALLAS,TX 75235

[2] UNIV TEXAS,SW MED CTR,DEPT PHARMACOL,DALLAS,TX 75235

[3] UNIV TEXAS,SW MED CTR,DEPT BIOCHEM,DALLAS,TX 75235

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1994年 / 238卷 / 04期

关键词：

G PROTEINS; GTP BINDING PROTEINS; SIGNAL TRANSDUCTION; X-RAY DIFFRACTION; PROTEIN CRYSTALLIZATION;

D O I：

10.1006/jmbi.1994.1320

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Several different crystal forms of Giα1 have been grown and analyzed. Crystals of native protein containing bound GTPγS belong to space group P3121 or P3221 with cell dimensions a, b = 80·6 Åand c = 106·3 Å and diffract to a resolution of 1·9 Å using synchrotron radiation. Crystals of native protein containing bound GDP belong to space group I4 with cell dimensions a, b = 121·3 Å, and c = 67·7 Å and diffract to 3·0Å. Data sets from crystals grown using mutant proteins have also been obtained and characterized. © 1994 Academic Press Limited.

引用

页码：630 / 634

页数：5

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[1] CRYSTAL-STRUCTURE OF ACTIVE ELONGATION-FACTOR TU REVEALS MAJOR DOMAIN REARRANGEMENTS [J].