Open AccessRecombinant bovine uteroglobin at 1.6 Å resolution: a preliminary X‐ray crystallographic analysis
Author(s) -
Von Der Decken Victoria,
Delbrück Heinrich,
Herrler Andreas,
Beier Henning M.,
Fischer Rainer,
Hoffmann Kurt M. V.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105011231
Subject(s) - crystallography , recombinant dna , uteroglobin , chemistry , resolution (logic) , biochemistry , gene , artificial intelligence , computer science
Uteroglobin (UG) is a conserved protein which is induced by progesterone and secreted by the epithelia of various mammalian reproductive and respiratory organs. Recombinant bovine uteroglobin (recbUG), consisting of 80 amino acids with a C‐terminal His 6 tag, was overexpressed in Escherichia coli and purified. The protein was crystallized in two geometric forms, rhomboid and cuneate (wedge‐shaped), by the hanging‐drop vapour‐diffusion method at 295 K. The rhomboid crystals diffracted to a maximum resolution of 1.6 Å using synchrotron radiation. These crystals belong to space group P 2 1 2 1 2, with unit‐cell parameters a = 81.42, b = 82.82, c = 45.26 Å, and contain four monomers per asymmetric unit. The cuneate crystals diffracted to 2.35 Å resolution using a rotating‐anode generator. These crystals belong to space group C 222 1 , with unit‐cell parameters a = 43.39, b = 93.94, c = 77.30 Å, and contain two molecules per asymmetric unit.