Thermophilic alcohol dehydrogenase from the mesophile Entamoeba histolytica: crystallization and preliminary X-ray characterization.
The tetrameric NADP(+)-dependent secondary alcohol dehydrogenase from Entamoeba histolytica has been crystallized in its apo form. The crystals belong to space group C222(1), with unit-cell parameters a = 76.89, b = 234.24, c = 96.24 A, and diffract to 1.9 A at liquid-nitrogen temperature. Analysis of the Patterson self-rotation function shows that the crystals contain one dimer per asymmetric unit.
Shimon
Linda J W
LJ
Department of Chemical Services, The Weizmann Institute of Science, Rehovot 76100, Israel. linda.shimon@weizmann.ac.il
Peretz
Moshe
M
Goihberg
Edi
E
Burstein
Yigal
Y
Frolow
Felix
F
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004748:Entamoeba histolytica / Q000737:chemistry / Q000201:enzymology*; D011487:Protein Conformation
D000426:Alcohol Dehydrogenase