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结晶设置过程中的温度对金属内肽酶沉淀形成和晶体形状的影响。

Influence of temperature during crystallization setup on precipitate formation and crystal shape of a metalloendopeptidase.

作者信息

Bogdanović Xenia, Hinrichs Winfried

机构信息

Department of Molecular Structural Biology, Institute for Biochemistry, Ernst-Moritz-Arndt University, Greifswald, Germany.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt 3):421-3. doi: 10.1107/S1744309111001783. Epub 2011 Feb 25.

DOI:10.1107/S1744309111001783
PMID:21393857
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3053177/
Abstract

It is well known that protein crystallization is affected by several different parameters such as the composition of the reservoir solution, the protein concentration, the pH and the temperature. An effect of different temperatures during setup of crystallization experiments was observed for a metalloendopeptidase (AsaP1(E294A)). Spontaneous protein precipitation was reduced and the crystal shape could be improved by decreasing the temperature during crystallization setup.

摘要

众所周知，蛋白质结晶受多种不同参数的影响，如储液组成、蛋白质浓度、pH值和温度。对于一种金属内肽酶（AsaP1(E294A)），在结晶实验设置过程中观察到了不同温度的影响。通过在结晶设置过程中降低温度，可以减少蛋白质的自发沉淀，并改善晶体形状。

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本文引用的文献

1
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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jul 1;65(Pt 7):695-7. doi: 10.1107/S1744309109020132. Epub 2009 Jun 27.
2
The AsaP1 peptidase of Aeromonas salmonicida subsp. achromogenes is a highly conserved deuterolysin metalloprotease (family M35) and a major virulence factor.杀鲑气单胞菌无色亚种的AsaP1肽酶是一种高度保守的去铁素溶菌素金属蛋白酶（M35家族），也是一种主要的毒力因子。
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