Crystallization of the FaeE chaperone of Escherichia coli F4 fimbriae.

TitleCrystallization of the FaeE chaperone of Escherichia coli F4 fimbriae.
Publication TypeJournal Article
Year of Publication2005
AuthorsVan Molle, I., L. Buts, F. Coppens, L. Qiang, L. Wyns, R. Loris, J. Bouckaert, and H. De Greve
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume61
IssuePt 4
Pagination427-31
Date Published2005 Apr 1
ISSN1744-3091
KeywordsAdhesins, 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.
DOI10.1107/S1744309105008432
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID16511060
PubMed Central IDPMC1952412