大麦麦芽α-淀粉酶的结晶及高pI同工酶α-淀粉酶2的初步X射线衍射研究

Crystallization of barley malt alpha-amylases and preliminary x-ray diffraction studies of the high pI isozyme, alpha-amylase 2.

作者信息

Svensson B, Gibson R M, Haser R, Astier J P

机构信息

Department of Chemistry, Carlsberg Laboratory, Copenhagen, Denmark.

出版信息

J Biol Chem. 1987 Oct 5;262(28):13682-4.

PMID:3498717

Abstract

alpha-Amylase isozymes 1 and 2 isolated from germinated barley seeds have been crystallized by the hanging- or sitting-drop vapor diffusion technique. Crystals of alpha-amylase 2 suitable for x-ray diffraction analysis were grown at pH 6.7 and 22 degrees C from a solution of 1 mM calcium chloride, 10 mM MES, and 16% saturated ammonium sulfate. The space group is trigonal P3121 (or P3221) with unit cell dimensions a = b = 135.20 A, c = 79.63 A, and probably two molecules per asymmetric unit.

摘要

从发芽大麦种子中分离出的α-淀粉酶同工酶1和2，已通过悬滴或坐滴气相扩散技术结晶。适合X射线衍射分析的α-淀粉酶2晶体，是在pH 6.7和22℃条件下，从含有1 mM氯化钙、10 mM MES和16%饱和硫酸铵的溶液中生长得到的。空间群为三方晶系P3121（或P3221），晶胞参数a = b = 135.20 Å，c = 79.63 Å，每个不对称单元可能含有两个分子。