The Corynebacterium glutamicum aconitase repressor: scratching around for crystals

被引:3
作者
Garcia-Nafria, Javier [1 ]
Baumgart, Meike [2 ]
Bott, Michael [2 ]
Wilkinson, Anthony J. [1 ]
Wilson, Keith S. [1 ]
机构
[1] Univ York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, England
[2] Forschungszentrum Julich, Inst Biotechnol 1, D-52425 Julich, Germany
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
关键词
aconitase repressor; Corynebacterium glutamicum; heterogeneous nucleation; PROTEIN CRYSTALS; DIFFRACTION DATA; CRYSTALLIZATION; NUCLEATION; SURFACES;
D O I
10.1107/S1744309110029015
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Imperfections on the surfaces of crystallization containers are known to influence crystal formation and are thought to do so by helping to overcome the nucleation barrier. The intentional creation of imperfections has been widely applied to induce crystallization of small molecules, but has not been reported for protein crystallization. Here, the crystallization and preliminary X-ray analysis of the TetR-type aconitase repressor are reported. This regulator was the first transcription factor to be identified in the regulation of the tricarboxylic acid cycle in Corynebacterium glutamicum, an organism that is of special industrial interest and is an emerging model organism for Corynebacterineae. Successful crystallization involved introducing manual scratches on the surface of standard commercial plates, which led to a substantial improvement in crystal nucleation and quality.
引用
收藏
页码:1074 / 1077
页数:4
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