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小麦内源性α-淀粉酶抑制剂的晶体学研究

Crystallographic study of endogenous alpha-amylase inhibitor from wheat.

作者信息

Maeda K, Sato M, Kato Y, Tanaka N, Hata Y, Katsube Y, Matsubara H

出版信息

J Mol Biol. 1987 Feb 20;193(4):825-6. doi: 10.1016/0022-2836(87)90364-0.

DOI:10.1016/0022-2836(87)90364-0
PMID:3497278
Abstract

Endogenous alpha-amylase inhibitor from wheat has been crystallized by a microdialysis method. There are two forms of monoclinic crystal in a microdialysis cell with a space group of P2(1). The unit cell dimensions are a = 43.5 A, b = 64.8 A, c = 32.2 A, beta = 113 degrees for the rod-like crystal, and a = 42.5 A, b = 65.2 A, c = 32.2 A, beta = 112 degrees for the plate-like crystal. The former is suitable for structure analysis because it gives the sharp diffraction beyond 2.0 A resolution, and the latter tends to form a twin crystal. A heavy-atom derivative has been successfully prepared with the heavy-atom reagent K2PtCl4, and structure analysis is in progress.

摘要

从小麦中提取的内源性α-淀粉酶抑制剂已通过微透析法结晶。在空间群为P2(1)的微透析池中存在两种单斜晶形式。棒状晶体的晶胞参数为a = 43.5 Å,b = 64.8 Å,c = 32.2 Å,β = 113°;板状晶体的晶胞参数为a = 42.5 Å,b = 65.2 Å,c = 32.2 Å,β = 112°。前者适合进行结构分析,因为它能给出分辨率超过2.0 Å的清晰衍射图,而后者容易形成孪晶。已使用重原子试剂K2PtCl4成功制备了重原子衍生物,结构分析正在进行中。

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