番红花几丁质酶的分离、纯化、结晶及初步晶体学研究
Isolation, purification, crystallization and preliminary crystallographic studies of a chitinase from Crocus vernus.
作者信息
Akrem Ahmed, Iqbal Sadaf, Buck Friedrich, Meyer Arne, Perbandt Markus, Voelter Wolfgang, Betzel Christian
机构信息
Department of Chemistry, University of Hamburg, c/o DESY, Laboratory for Structural Biology of Infection and Inflammation, Notkestrasse 85, 22603 Hamburg, Germany.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt 3):340-3. doi: 10.1107/S1744309110053698. Epub 2011 Feb 23.
Abstract
A chitinase has been isolated and purified from Crocus vernus corms. N-terminal amino-acid sequence analysis of the approximately 30 kDa protein showed 33% identity to narbonin, a seed protein from Vicia narbonensis L. The C. vernus chitinase was crystallized by the hanging-drop vapour-diffusion method using PEG 8000 as the main precipitant. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a=172.3, b=37.1, c=126.4 Å, β=127° and two molecules per asymmetric unit. Diffraction data were collected to a resolution of 2.1 Å.
摘要
已从番红花球茎中分离并纯化出一种几丁质酶。对这种约30 kDa的蛋白质进行N端氨基酸序列分析，结果显示其与来自窄叶野豌豆的种子蛋白narbonin有33%的同源性。采用悬滴气相扩散法，以聚乙二醇8000作为主要沉淀剂，使番红花几丁质酶结晶。该晶体属于单斜空间群C2，晶胞参数为a = 172.3、b = 37.1、c = 126.4 Å，β = 127°，每个不对称单元中有两个分子。收集到了分辨率为2.1 Å的衍射数据。
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