Publication Type:Journal Article
Source:Acta Crystallographica Section D-Biological Crystallography, Volume 58, p.1901-1906 (2002)
DOI Name (links to online publication)10.1107/s0907444902016608
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.