Recombinant bovine uteroglobin at 1.6 Å resolution: a preliminary X-ray crystallographic analysis
Journal Article
·
· Acta Crystallographica. Section F
- Institute of Anatomy and Reproductive Biology, Medical School RWTH Aachen, Wendlingweg 2, 52074 Aachen (Germany)
- Institute for Molecular Biotechnology VII, Aachen University, Worringerweg 1, 52074 Aachen (Germany)
- Fraunhofer Institute for Molecular Biotechnology and Applied Ecology, Worringerweg 1, 52074 Aachen (Germany)
The crystallization of recombinant bovine uteroglobin. 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{sub 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 P2{sub 1}2{sub 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 C222{sub 1}, with unit-cell parameters a = 43.39, b = 93.94, c = 77.30 Å, and contain two molecules per asymmetric unit.
- OSTI ID:
- 22356005
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 5 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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