Purification, crystallization and preliminary X-ray analysis of Hsp33 from Saccharomyces cerevisiae.
The heat-shock protein Hsp33 from the yeast Saccharomyces cerevisiae has been overexpressed, purified and crystallized. A crystal was obtained using the hanging-drop vapour-diffusion method and a data set was collected to 2.7 A resolution. The crystal belongs to space group P4(3)2(1)2, with unit-cell parameters a = b = 96.43, c = 132.22 A, alpha = beta = gamma = 90 degrees . The asymmetric unit is assumed to contain two subunits of Hsp33, with a V(M) value of 2.96 A(3) Da(-1) and a solvent content of 58.41%.
Liu
Wei
W
Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China.
Zhou
Ye-Yun
YY
Teng
Mai-Kun
MK
Zhou
Cong-Zhao
CZ
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D006360:Heat-Shock Proteins; D029701:Saccharomyces cerevisiae Proteins