重组人骨生成蛋白-1（hOP-1）的结晶及初步晶体学数据

Crystallization and preliminary crystallographic data of recombinant human osteogenic protein-1 (hOP-1).

作者信息

Griffith D L, Oppermann H, Rueger D C, Sampath T K, Tucker R F, Carlson W D

机构信息

Brandeis University Rosenstiel Basic Medical Sciences Research Center, Waltham, MA 02254.

出版信息

J Mol Biol. 1994 Dec 16;244(5):657-8. doi: 10.1006/jmbi.1994.1761.

DOI:10.1006/jmbi.1994.1761

PMID:7990148

Abstract

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.

摘要

我们获得了重组人骨生成蛋白-1（hOP-1）的三角晶体，hOP-1是转化生长因子-β（TGF-β）超家族的成员。hOP-1（也称为骨形态发生蛋白-7，BMP-7）是一种骨形态发生蛋白，以M(r) 32至36 kDa的二聚体形式具有活性。晶体具有空间群P3(1)21或对映体P3(2)21的对称性，晶胞参数为a = b = 99.46 Å，c = 42.09 Å。晶体衍射分辨率达到2.2 Å，每个不对称单元中有一个hOP-1单体。在本文中，我们描述了骨形态发生蛋白的首次结晶，并给出了天然蛋白和两种重原子衍生物的初步X射线衍射数据结果。