PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF SWEET-POTATO BETA-AMYLASE

被引:10
作者
CUDNEY, R
MCPHERSON, A
机构
[1] Department of Biochemistry, University of California at Riverside, Riverside
关键词
BETA-AMYLASE; X-RAY; PROTEIN STRUCTURE; CRYSTALS;
D O I
10.1006/jmbi.1993.1026
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
Beta amylase from sweet potato has been crystallized in a form suitable for high resolution X-ray diffraction analysis from a mixture of polyethylene glycol 400 and ammonium sulfate at room temperature. The crystals are rectangular prisms and occasionally reach a size of 1 mm on an edge. The space group of the crystals is I422 with cell dimensions of a = b = 196.4 AÅ and c = 72.2 AÅ. There are four tetramers of about Mr = 210,000 in the unit cell centered at 222 symmetry points. The asymmetric unit is a single beta amylase subunit of about Mr = 52,000. The tetrameric molecule must have exact 222 molecular symmetry relating its subunits. © 1993 Academic Press, Inc.
引用
收藏
页码:253 / 254
页数:2
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