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卵清蛋白和扁白蛋白单晶的初步X射线分析。

Preliminary x-ray analysis of single crystals of ovalbumin and plakalbumin.

作者信息

Miller M, Weinstein J N, Wlodawer A

出版信息

J Biol Chem. 1983 May 10;258(9):5864-6.

PMID:6853552
Abstract

Two crystal forms of hen ovalbumin have been grown and were characterized by x-ray diffraction. Crystals of ovalbumin grown at pH 5.4 are monoclinic, belonging to the space group C2 (a = 116.5 A, b = 41.8 A, c = 70.5 A, beta = 101.5 degrees). At pH 5.8 or higher ovalbumin forms triclinic crystals of space group P1 (a = 62.0 A, b = 84.3 A, c = 72.2 A, alpha = 87.4 degrees, beta = 103.9 degrees, gamma = 108.7 degrees). These crystals are usually small and difficult to grow reproducibly. Crystals of plakalbumin (a proteolytic modification of ovalbumin) are much easier to grow and appear suitable for three-dimensional structure determination. Their space group is C2 (a = 99.9 A, b = 102.0 A, c = 79.3 A, beta = 112.1 degrees) with two plakalbumin molecules in each asymmetric unit.

摘要

已培养出两种鸡卵清蛋白晶体形式,并通过X射线衍射对其进行了表征。在pH 5.4条件下生长的卵清蛋白晶体为单斜晶系,属于空间群C2(a = 116.5 Å,b = 41.8 Å,c = 70.5 Å,β = 101.5°)。在pH 5.8或更高时,卵清蛋白形成空间群为P1的三斜晶系晶体(a = 62.0 Å,b = 84.3 Å,c = 72.2 Å,α = 87.4°,β = 103.9°,γ = 108.7°)。这些晶体通常较小且难以重复生长。副白蛋白(卵清蛋白的一种蛋白水解修饰产物)晶体更容易生长,似乎适合用于三维结构测定。其空间群为C2(a = 99.9 Å,b = 102.0 Å,c = 79.3 Å,β = 112.1°),每个不对称单元中有两个副白蛋白分子。

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