Crystallization and preliminary diffraction studies of the RNA polymerase subunit RPB5 from Saccharomyces cerevisiae.
Crystals of the RNA polymerase subunit RPB5 from Saccharomyces cerevisiae have been obtained by vapour-diffusion techniques. The protein has been overexpressed in bacterial cells as a fusion with glutathione S-transferase. Two monoclinic crystal forms can be grown under different sets of conditions. In both cases, the diffraction is consistent with space group P21, with unit-cell parameters a = 45. 3, b = 135.3, c = 47.3 A, beta = 118.6 degrees for crystal form I and a = 48.4, b = 137.1, c = 47.1 A, beta = 118.6 degrees for crystal form II.
Hodach
M
M
Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7, England.
Todone
F
F
Eloranta
J J
JJ
Onesti
S
S
Weinzierl
R O
RO
D003460:Crystallization; D018360:Crystallography, X-Ray; D011994:Recombinant Proteins / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D011994:Recombinant Proteins