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Crystallization of protein–protein complexes
Author(s) -
Radaev Sergei,
Sun Peter D.
Publication year - 2002
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889802013973
Subject(s) - crystallization , protein crystallization , ammonium sulfate , chemistry , limiting , polyethylene glycol , crystallography , salt (chemistry) , peg ratio , protein data bank , protein structure , chromatography , biochemistry , organic chemistry , mechanical engineering , finance , economics , engineering
Crystallizing protein–protein complexes remains a rate‐limiting step in their structure characterization. Crystallization conditions for the known protein–protein complexes have been surveyed in both the Protein Data Bank and the BMCD database. Compared with non‐complexed proteins, crystallization conditions for protein–protein complexes are less diverse and heavily favor (71% versus 27%) polyethylene glycols (PEG) rather than ammonium sulfate or other high‐salt crystallization conditions. The results suggest that the stability of protein complexes limits their available crystallization configuration space. Based on the survey, a set of sparse‐matrix screen conditions was designed.