Crystal parameters of an alcohol dehydrogenase from the extreme thermophile Thermoanaerobium brockii.
A bacterial thermophilic alcohol dehydrogenase which is stable and active at 85 degrees C, has been crystallized by vapor diffusion from solutions of polyethylene glycol. A monoclinic crystal form diffracts to 2.8 A resolution and belongs to space group C2 with unit cell dimensions a = 139.0 A, b = 137.4 A, c = 80.9 A and beta = 93.23 degrees. The asymmetric unit contains four molecules which exhibit 222 point symmetry. A second crystal form is orthohombic, space group P2(1)2(1)2 with unit cell dimensions a = 168.0 A, b = 123.0 A, c = 80.0 A, and it diffracts to 3.2 A resolution.
Zhang
Z
Z
Case Western Reserve University, School of Medicine, Department of Biochemistry, Cleveland, Ohio 44106-4935.
Djebli
A
A
Shoham
M
M
Frolow
F
F
Peretz
M
M
Burstein
Y
Y
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D001421:Bacteria, Anaerobic / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry; D003461:Crystallography; D006358:Hot Temperature; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D000426:Alcohol Dehydrogenase