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Preliminary crystallographic analysis of an enzyme involved in erythromycin biosynthesis: Cytochrome P450eryF
Author(s) -
CuppVickery Jill R.,
Li Huiying,
Poulos Thomas L.
Publication year - 1994
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.340200210
Subject(s) - orthorhombic crystal system , crystallography , polyethylene glycol , chemistry , substrate (aquarium) , cytochrome , molecule , enzyme , yield (engineering) , stereochemistry , cytochrome b5 , escherichia coli , materials science , biochemistry , crystal structure , biology , organic chemistry , gene , ecology , metallurgy
Cytochrome P450eryF was overexpressed in Escherichia coli and purified in high yield. Crystals of the protein in the presence of the substrate, 6‐deoxyerythronolide B, have been obtained by the hanging drop vapor diffusion method, using polyethylene glycol 4000 as a precipitant. The crystals belong to the orthorhombic space group P 2 1 2 1 2 1 with unit cell dimensions of a = 54.16 Å, b = 79.67 Å, and c = 99.48 Å and one molecule per asymmetric unit. A complete native data set has been collected to a resolution of 2.1 Å, and anomalous dispersion difference Patterson maps have revealed the location of the single heme iron atom. © 1994 Wiley‐Liss, Inc.