Crystallization of the secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus 39E.
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
---|---|
Data(s) |
20/05/2014
20/05/2014
01/12/1996
|
Resumo |
The secondary alcohol dehydrogenase from the thermophile Thermoanaerobacter ethanolicus 39E has been crystallized at 40 degrees C by vapour difussion using polyethelene glycol as a precipitant. The orthorhombic crystals belong to the space group P 2(1)2(1)2 with cell constants of a=170.0 Angstrom, b=125.7 Angstrom and c=80.5 Angstrom. A native X-ray diffraction data set has been collected to 2.7 Angstrom resolution. |
Formato |
423-426 |
Identificador |
Protein and Peptide Letters. Schiphol: Bentham Science Publ Bv, v. 3, n. 6, p. 423-426, 1996. 0929-8665 http://hdl.handle.net/11449/39063 WOS:A1996VW06200010 |
Idioma(s) |
eng |
Publicador |
Bentham Science Publ Bv |
Relação |
Protein and Peptide Letters |
Direitos |
closedAccess |
Tipo |
info:eu-repo/semantics/article |