Hm. Baker et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES ON CYTOSOLIC (CLASS-1) ALDEHYDE DEHYDROGENASE FROM SHEEP LIVER, Journal of Molecular Biology, 241(2), 1994, pp. 263-264
The cytosolic (Class 1) aldehyde dehydrogenase (AIDH) from sheep liver
has been crystallized in a form suitable for X-ray diffraction studie
s. The crystals, grown by vapour diffusion using 6.5 to 7.5% methoxypo
lyethylene glycol 5000 as precipitant, at pH 6.5, are orthorhombic wit
h cell dimensions a = 80.7, b = 92.5, c = 151.6 a, space-group P2(1)2(
1)2(1), and one dimer in the asymmetric unit;. The crystals diffract t
o at least 2.8 Angstrom resolution. Although unmodified AIDH crystalli
zed readily, a key factor in obtaining diffraction-quality crystals wa
s the covalent attachment of an active site reporter group, provided b
y -dihydro-3-methyl-6-nitro-2H-1,3-benzoxazin-2-one.