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-beta (TGF-beta) 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(1)21 or the enantiomorph P3(2)21 with unit cell dimensions of a = b = 99.46 A, c = 42.09 A. The crystals diffract to 2.2 A 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.
Griffith
D L
DL
Brandeis University Rosenstiel Basic Medical Sciences Research Center, Waltham, MA 02254.
Oppermann
H
H
Rueger
D C
DC
Sampath
T K
TK
Tucker
R F
RF
Carlson
W D
WD
D055419:Bone Morphogenetic Protein 7; D019485:Bone Morphogenetic Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D016212:Transforming Growth Factor beta / Q000737:chemistry
C525819:BMP7 protein, human; D055419:Bone Morphogenetic Protein 7; D019485:Bone Morphogenetic Proteins; D011506:Proteins; D011994:Recombinant Proteins; D016212:Transforming Growth Factor beta