Crystallization of mutant beta subunit of F1-ATPase from thermophilic Bacillus PS3.
The mutant beta subunit of F1-ATPase from a thermophilic Bacillus strain, PS3, in which tyrosine at position 341 is replaced by leucine (beta Y341L) was expressed in Escherichia coli and crystallized by the vapor-diffusion procedure. Small needle-like crystals were obtained using ammonium sulfate as a precipitant and grown by the stepwise seeding method. The crystals obtained by this procedure diffracted X-rays to about 3 A resolution. The diffraction patterns indicated that the crystals belong to the orthorhombic system and the space group I222 or I2(1)2(1)2(1) with unit-cell dimensions of a = 232 A, b = 66 A, and c = 80 A. It is thought that the asymmetric unit comprises one beta Y341L molecule.
Saika
K
K
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.
Inaka
K
K
Matsui
T
T
Yoshida
M
M
Miki
K
K
D001407:Bacillus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D006180:Proton-Translocating ATPases