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Preliminary X-ray crystallographic studies on alcohol dehydrogenase from Drosophila.

Abstract：

:The alcohol dehydrogenase (ADHase) enzyme catalyses the oxidation of alcohols to aldehydes or ketones using NAD+ as a cofactor. Functional ADHase from Drosophila lebanonensis is a dimer, with a monomeric molecular weight of 27,000 and with 254 residues in each polypeptide chain. Crystals of the protein have been grown with and without NAD+. Two crystal forms have been observed. Most crystals are plate-like, 0.05 mm in their shortest dimension and up to 0.4 mm in their longest dimension. These crystals are generally too small to diffract efficiently using conventional X-ray sources, so preliminary studies were carried out using the Synchrotron Radiation Source at the SERC Daresbury Laboratory. Twinning was a severe problem with this crystal form. The second form is grown in the absence of NAD+ but with DL-dithiothreitol present. These crystals grow more evenly and diffract to better than 2 A resolution. They are monoclinic, with cell dimensions, a = 81.24(6) A, b = 55.75(4) A, c = 109.60(7) A and beta = 94.26(9) degrees, space group P2(1). There are two dimers in the asymmetric unit, but at low resolution a rotated cell with one dimer per asymmetric unit can be obtained.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Gordon EJ,Bury SM,Sawyer L,Atrian S,Gonzalez-Duarte R

doi

10.1016/0022-2836(92)90705-o

keywords:

subject

Has Abstract

pub_date

1992-09-05 00:00:00

pages

356-8

issue

1

eissn

0022-2836

issn

1089-8638

pii

0022-2836(92)90705-O

journal_volume

227

pub_type

杂志文章

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