Crystallization and preliminary X-ray diffraction studies of undecaprenyl diphosphate synthase from Micrococcus luteus B-P 26.
Undecaprenyl diphosphate synthase from Micrococcus luteus B-P 26, one of the Z-prenyl chain-elongating enzymes, was crystallized using the sitting-drop vapour-diffusion method with ammonium sulfate and lithium sulfate as precipitants. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 127.2, b = 60.2, c = 75.7 A, beta = 105.6 degrees. The crystals diffract X-rays to at least 2.2 A resolution using synchrotron radiation and are suitable for high-resolution crystal structure analysis.
Fujihashi
M
M
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Shimizu
N
N
Zhang
Y W
YW
Koyama
T
T
Miki
K
K
D019883:Alkyl and Aryl Transferases / Q000737:chemistry* / Q000302:isolation & purification; D000645:Ammonium Sulfate; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D004058:Diffusion; D018020:Lithium Compounds; D016982:Micrococcus luteus / Q000201:enzymology*; D013431:Sulfates; D014835:Volatilization; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D018020:Lithium Compounds; D013431:Sulfates; C054097:lithium sulfate; D019883:Alkyl and Aryl Transferases; C023266:undecaprenyl pyrophosphate synthetase; D000645:Ammonium Sulfate