The prospects of protein nanocrystallography

被引:50
作者
Bodenstaff, ER
Hoedemaeker, FJ
Kuil, ME
de Vrind, HPM
Abrahams, JP
机构
[1] Leiden Univ, Dept Biophys & Struct Chem, NL-2300 RA Leiden, Netherlands
[2] KeyDP BV, NL-2300 AB Leiden, Netherlands
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷
关键词
D O I
10.1107/S0907444902016608
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The miniaturization of protein crystallography's experimental method has several advantages. Firstly, it reduces the amount of protein required for identifying crystallization conditions, allowing crystallographic studies of rare natural proteins and complexes. Secondly, higher levels of supersaturation can be obtained in very small volumes, allowing the exploration of additional crystallization conditions. Thirdly, there are indications that protein crystals grown in very small volumes may be better ordered. Fourthly, miniaturization and automation go hand in hand, opening the prospects of easier and more reproducible experimentation. Progress in the development of nanocrystallography is discussed and the remaining bottlenecks are highlighted.
引用
收藏
页码:1901 / 1906
页数:6
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