Open AccessCrystallization and preliminary crystallographic analysis of Gre2p, an NADP + ‐dependent alcohol dehydrogenase from Saccharomyces cerevisiae
Author(s) -
Breicha Klaus,
Müller Marion,
Hummel Werner,
Niefind Karsten
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110018889
Subject(s) - alcohol dehydrogenase , crystallization , saccharomyces cerevisiae , crystallography , alcohol , chemistry , materials science , biochemistry , yeast , organic chemistry
Gre2p [ G enes de r espuesta a e stres (stress‐response gene)] from Saccharomyces cerevisiae is a monomeric enzyme of 342 amino acids with a molecular weight of 38.1 kDa. The enzyme catalyses both the stereospecific reduction of keto compounds and the oxidation of various hydroxy compounds and alcohols by the simultaneous consumption of the cofactor NADPH and formation of NADP + . Crystals of a Gre2p complex with NADP + were grown using PEG 8000 as a precipitant. They belong to the monoclinic space group P 2 1 . The current diffraction resolution is 3.2 Å. In spite of the monomeric nature of Gre2p in solution, packing and self‐rotation calculations revealed the existence of two Gre2p protomers per asymmetric unit related by a twofold noncrystallographic axis.