Crystallization and Preliminary Crystallographic Data of Recombinant Human Osteogenic Protein-1 (hOP-1)
We have obtained trigonal crystals of recombinant human osteogenic protein-1 (hOP-1), a member of the transforming growth factor-β: (TGF-β) superfamily. hOP-1 (also referred to as BMP-7) is a bone morphogenetic protein and is active as a dimer of M r 32 to 36 kDa. The crystals have the symmetry of s...
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Veröffentlicht in: | Journal of molecular biology 1994-12, Vol.244 (5), p.657-658 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | We have obtained trigonal crystals of recombinant human osteogenic protein-1 (hOP-1), a member of the transforming growth factor-β: (TGF-β) superfamily. hOP-1 (also referred to as BMP-7) is a bone morphogenetic protein and is active as a dimer of
M
r 32 to 36 kDa. The crystals have the symmetry of space group
P3
121 or the enantiomorph
P 3
221 with unit cell dimensions of
a =
b = 99.46 Å,
c = 42.09 Å. The crystals diffract to 2.2 Å resolution and there is one hOP-1 monomer per asymmetric unit. In this paper we describe the first crystallization of a bone morphogenetic protein and present the results of preliminary X-ray diffraction data from the native protein and two heavy-atom derivatives. |
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ISSN: | 0022-2836 1089-8638 |
DOI: | 10.1006/jmbi.1994.1761 |