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
Hauptverfasser: Griffith, Diana L., Oppermann, Hermann, Rueger, David C., Sampath, T.Kuber, Tucker, Ronald F., Carlson, William D.
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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.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.1994.1761