CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE CAMP-DEPENDENT PROTEIN-KINASE CATALYTIC SUBUNIT FROM SACCHAROMYCES-CEREVISIAE

被引：10
|
作者：
KURET, J
PFLUGRATH, JW
机构：
[1] Cold Spring Harbor Laboratory, Cold Spring Harbor
来源：
BIOCHEMISTRY | 1991年 / 30卷 / 43期
关键词：
D O I：
10.1021/bi00107a031
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：
A truncated variant of TPK1, the yeast cAMP-dependent protein kinase catalytic subunit, was overexpressed in an engineered strain of Saccharomyces cerevisiae, purified by liquid chromatography, and crystallized from solutions of 2-propanol and magnesium at alkaline pH. The crystals are hexagonal dipyramids, space group P6(1)22 (P6(5)22), with unit-cell parameters a = b = 61 angstrom, c = 320 angstrom. Large single crystals suitable for diffraction analysis are obtainable by microseeding, and diffract beyond 2.8-angstrom resolution. Crystal density measurements reveal 12 kinase monomers per unit cell with a single kinase monomer per asymmetric unit.
引用
收藏
页码：10595 / 10600
页数：6
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