Title | Crystallization of the FaeE chaperone of Escherichia coli F4 fimbriae. |
Publication Type | Journal Article |
Year of Publication | 2005 |
Authors | Van Molle, I., L. Buts, F. Coppens, L. Qiang, L. Wyns, R. Loris, J. Bouckaert, and H. De Greve |
Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun |
Volume | 61 |
Issue | Pt 4 |
Pagination | 427-31 |
Date Published | 2005 Apr 1 |
ISSN | 1744-3091 |
Keywords | Adhesins, Escherichia coli, Crystallization, Escherichia coli Proteins, Fimbriae, Bacterial, Molecular Chaperones, Multiprotein Complexes, Selenomethionine, X-Ray Diffraction |
Abstract | F4 (formerly K88) fimbriae from enterotoxigenic Escherichia coli are assembled via the FaeE/FaeD chaperone/usher pathway. The chaperone FaeE crystallizes in three crystal forms, all belonging to space group C2. Crystals of form 1 diffract to 2.3 A and have unit-cell parameters a = 195.7, b = 78.5, c = 184.6 A, beta = 102.2 degrees. X-ray data for crystal form 2 were collected to 2.7 A using an SeMet variant of FaeE. The crystals have unit-cell parameters a = 136.4, b = 75.7, c = 69.4 A, beta = 92.8 degrees. Crystals of form 3 were formed in a solution containing the FaeE-FaeG complex and diffract to 2.8 A. Unit-cell parameters are a = 109.7, b = 78.6, c = 87.8 A, beta = 96.4 degrees. |
DOI | 10.1107/S1744309105008432 |
Alternate Journal | Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |
PubMed ID | 16511060 |
PubMed Central ID | PMC1952412 |
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