It's all in the crystals ...

被引：31

作者：

Derewenda, Zygmunt S. ^{[1
]}

机构：

[1] Univ Virginia, Dept Mol Physiol & Biol Phys, Charlottesville, VA 22908 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2011年 / 67卷

关键词：

RATIONAL PROTEIN CRYSTALLIZATION; SURFACE ENTROPY REDUCTION; STRUCTURAL BASIS; RECOGNITION; MUTATIONS; BACE-1; HIV-1; INTERFACES; INHIBITORS; RESOLUTION;

D O I：

10.1107/S0907444911007797

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Macromolecular crystallography relies on the availability and quality of single crystals; these are typically obtained through extensive screening, which has a very low intrinsic success rate. Crystallization is not a completely stochastic process and many proteins do not succumb to crystallization because of specific microscopic features of their molecular surfaces. It follows that rational surface engineering through site-directed mutagenesis should allow a systematic and significant improvement in crystallization success rates. Here, one such established strategy, surface-entropy reduction (SER), is discussed, including its successes, limitations and possible future developments.

引用

页码：243 / 248

页数：6

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