| Literature DB >> 12393920 |
E Rene Bodenstaff1, Flip J Hoedemaeker, Maxim E Kuil, Hans P M de Vrind, Jan Pieter Abrahams.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2002 PMID: 12393920 DOI: 10.1107/s0907444902016608
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449