Crystallization of the FaeE chaperone of Escherichia coli F4 fimbriae.
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.
Van Molle
Inge
I
Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussel, Belgium. ivmolle@vub.ac.be
Buts
Lieven
L
Coppens
Fanny
F
Qiang
Liu
L
Wyns
Lode
L
Loris
Remy
R
Bouckaert
Julie
J
De Greve
Henri
H
D018830:Adhesins, Escherichia coli / Q000737:chemistry; D003460:Crystallization / Q000379:methods; D029968:Escherichia coli Proteins / Q000737:chemistry*; D010861:Fimbriae, Bacterial / Q000737:chemistry; D018832:Molecular Chaperones / Q000737:chemistry*; D046912:Multiprotein Complexes / Q000737:chemistry; D012645:Selenomethionine; D014961:X-Ray Diffraction
D018830:Adhesins, Escherichia coli; D029968:Escherichia coli Proteins; C494388:FaeG protein, E coli; D018832:Molecular Chaperones; D046912:Multiprotein Complexes; C070012:faeE protein, E coli; D012645:Selenomethionine