Crystallization and preliminary crystallographic analysis of the NAD(H)-binding domain of Escherichia coli transhydrogenase.
Transhydrogenase is a proton-pumping membrane protein that is required for the cellular regeneration of NADPH. The NAD(H)-binding domain (domain I) of transhydrogenase from Escherichia coli was crystallized using the hanging-drop vapour-diffusion technique at room temperature. The crystals, which were grown from PEG 4000 and ammonium acetate in citrate buffer, belong to the triclinic space group P1, with unit-cell parameters a = 38.8, b = 66.8, c = 76.4 A, alpha = 67.5, beta = 80.8, gamma = 81.5 degrees. X-ray diffraction data were collected to 1.9 A resolution using synchrotron radiation. The crystals contain one dimer of transhydrogenase domain I per asymmetric unit.
Oswald
Christine
C
Department of Chemistry and Bioscience, Chalmers University of Technology, PO Box 462, SE-405 30 Göteborg, Sweden.
Johansson
Tomas
T
Törnroth
Susanna
S
Okvist
Mats
M
Krengel
Ute
U
D001665:Binding Sites; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins / Q000737:chemistry*; D009243:NAD / Q000737:chemistry; D009250:NADP Transhydrogenases / Q000737:chemistry*
D029968:Escherichia coli Proteins; D009243:NAD; D009250:NADP Transhydrogenases