Recombinant bovine uteroglobin at 1.6 Å resolution: a preliminary X-ray crystallographic analysis
- 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, Vol. 61, Issue Pt 5; Other Information: PMCID: PMC1952310; PMID: 16511079; PUBLISHER-ID: en5113; OAI: oai:pubmedcentral.nih.gov:1952310; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Crystallization and initial X-ray diffraction studies of scaffolding protein (gp7) of bacteriophage ϕ29
Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine β-lactoglobulin allergen