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Preliminary crystallographic analysis of class 3 rat liver aldehyde dehydrogenase
Author(s) -
Rose John P.,
Hempel John,
Kuo Ingrid,
Lindahl Ronald,
Wang BiCheng
Publication year - 1990
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340080404
Subject(s) - aldehyde dehydrogenase , class (philosophy) , aldehyde , crystallography , chemistry , stereochemistry , biochemistry , computational biology , biology , computer science , enzyme , artificial intelligence , catalysis
Abstract NAD‐linked aldehyde dehydrogenases (A1DH) (EC 1.2.1.3) catalyze the irreversible oxidation of a wide variety of aldehydes to their respective carboxylic acids. Crystals of a class 3 A1DH (from an Escherichia coli expression system) suitable for X‐ray analysis have been obtained. These crystals, which can be grown to a size of 0.8 × 0.3 × 0.2 mm, diffract to 2.5 Å resolution. Analysis of the diffraction pattern indicates that the crystals belong to the monoclinic space group P 2 1 , with cell parameters a = 65.11 Å, b = 170.67 Å, c = 47.15 Å, and β = 110.5°. Assuming one dimer per asymmetric unit, the value V m is calculated to be 2.45 and the solvent content of the crystal is estimated to be 50%. A self‐rotation function study produced significant rotation peaks (58% of the origin) on the K = 180 section at ψ = 90° and ϕ = 71° and 341°, indicating that the pseudo‐dimer axis is (or is very nearly) perpendicular to the b ‐axis.