Crystallization and preliminary X-ray diffraction study of the nickel-binding protein NikA of Escherichia coli.
NikA, a periplasmic nickel-binding protein involved in nickel-repellent chemotaxis has been crystallized. The crystals are hexagonal with space group P6(2) (or its enantiomorph) with a = 160.3 A and c = 138.4 A and they diffract to at least 3.0 A resolution in the laboratory. NikA presents sequence homology with several periplasmic solute-binding proteins from Gram-negative bacteria.
Charon
M H
MH
Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale J. P. Ebel CEA-CNRS, Grenoble, France.
Wu
L F
LF
Piras
C
C
de Pina
K
K
Mandrand-Berthelot
M A
MA
Fontecilla-Camps
J C
JC
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins; D009532:Nickel / Q000378:metabolism*
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C089849:nikA protein, E coli; D009532:Nickel