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CRYSTALLIZATION AND PRELIMINARY-ANALYSIS OF ENZYME-SUBSTRATE COMPLEXES OF PYRUVATE-KINASE FROM RABBIT MUSCLE

被引：6
作者：
SCHMIDTBASE, K
BUCHBINDER, JL
REED, GH
RAYMENT, I
机构：
[1] UNIV WISCONSIN,INST ENZYME RES,GRAD SCH,1710 UNIV AVE,MADISON,WI 53705
[2] UNIV WISCONSIN,COLL AGR & LIFE SCI,DEPT BIOCHEM,MADISON,WI 53705
来源：
PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1991年 / 11卷 / 02期
关键词：
PYRUVATE KINASE; CRYSTALS; ELECTRON PARAMAGNETIC RESONANCE; OXALATE; PYRUVATE;
D O I：
10.1002/prot.340110208
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：
Pyruvate kinase from rabbit muscle has been crystallized in a form suitable for high resolution X-ray analysis. Complexes of the enzyme with Mn2+ and either pyruvate or oxalate crystallize from solutions of polyethyleneglycol 8000 at pH 6.0. Crystals obtained from solutions of the complexes with pyruvate or oxalate appear isomorphous and belong to the triclinic space group P1. The crystals have unit cell dimensions a = 83.3(4) angstrom, b = 109.4(6) angstrom, c = 145.7(7) angstrom, alpha = 94.9-degrees, beta = 93.6-degrees, gamma = 112.2-degrees. These crystals diffract to better than 2.4 angstrom resolution and are stable in the X-ray beam for at least 20 hr. Electron paramagnetic resonance measurements on a single crystal show that Mn2+ is bound to the crystalline protein.
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收藏
页码：153 / 157
页数：5
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