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Crystallization of the chaperone protein SecB
Author(s) -
Vrielink Alice,
Beamer Lesa,
Le Thanh,
Eisenberg David
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560040824
Subject(s) - periplasmic space , crystallization , crystallography , chaperone (clinical) , polyethylene glycol , escherichia coli , monoclinic crystal system , biophysics , chemistry , protein crystallization , crystal structure , biochemistry , biology , gene , organic chemistry , medicine , pathology
The secretory protein SecB found in Escherichia coli is a molecular chaperone that binds to precursor forms of a number of proteins targeted for export to the periplasmic space. SecB maintains these proteins in a translocation‐competent conformation facilitating the translocation process. The material has been cloned and expressed in E. coli . Crystals have been grown from polyethylene glycol 8000 by vapor diffusion using the hanging drop technique. These crystals are monoclinic, belonging to space group C2 with unit cell dimensions a = 56.0 Å, b = 111.1 Å, c = 134.7 Å, and β = 104°. The crystals diffract to 8 Å resolution on a Rigaku imaging plate detector. Dynamic light scattering experiments suggest that SecB exhibits aggregation behavior with a number of different precipitating agents. These results may explain resistance of SecB to forming ordered crystals.