Methods for separating nucleation and growth in protein crystallisation

被引：67

作者：

Chayen, NE ^{[1
]}

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Div Biomed Sci, Biol Struct & Funct Sect, London SW7 2AZ, England

来源：

PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY | 2005年 / 88卷 / 03期

关键词：

microbatch; nucleation; phase diagrams; protein crystallisation; vapour diffusion;

D O I：

10.1016/j.pbiomolbio.2004.07.007

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The availability of high-quality crystals is crucial to the structure determination of proteins by X-ray diffraction. With the advent of structural genomics the pressure to produce crystals is greater than ever before. Finding favourable conditions for crystallisation. is usually achieved by screening of the protein solution with numerous crystallising agents. Optimisation of the crystallisation conditions involves the manipulation of the crystallisation phase diagram with the aim of leading crystal growth in the direction that will produce the desired results. This article highlights recent advances in experimental methods for improving crystal size and quality by separating the nucleation and growth phases of crystallisation using the vapour diffusion and microbatch techniques. (c) 2004 Elsevier. Ltd. All rights reserved.

引用

页码：329 / 337

页数：9

共 28 条

[1] PROTEIN CRYSTAL-GROWTH - AN APPROACH BASED ON PHASE-DIAGRAM DETERMINATION [J].