Crystallization and preliminary X-ray diffraction analysis of proximal thread matrix protein 1 (PTMP1) from Mytilus galloprovincialis.
Crystallization and preliminary X-ray diffraction analysis of proximal thread matrix protein 1 (PTMP1) from Mytilus galloprovincialis.
复制标题
贻贝近端丝基质蛋白 1 (PTMP1) 的结晶和初步 X 射线衍射分析
DOI：
10.1107/s2053230x14006165
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
M. Gertz
中科院分区：
文献类型：
--
作者：
M.H. Suhre;T. Scheibel;C. Steegborn;M. Gertz
为了适应不断变化的海洋环境，蓝贻贝通过它们的胶原纤维附着在各种表面上。PTMP1（近端丝基质蛋白1）是一种已鉴定的存在于近端丝中的基质蛋白，能够与胶原蛋白结合。其序列包含两个血管性血友病因子A型样重复序列。为了表征PTMP 1的结构和结构域架构，重组蛋白通过气相扩散结晶。晶体的衍射分辨率为1.95 μ m，空间群为P21，晶胞参数a = 62.0，B = 62.3，c = 122.6 μ m，β = 102.2°。 马修斯系数表明在不对称单元中存在两个单体，溶剂含量为48.3%。
In order to deal with the dynamic ocean environment, blue mussels adhere to various surfaces via their collagenous byssal threads. PTMP1 (proximal thread matrix protein 1) is one identified matrix protein residing in the proximal thread and is capable of collagen binding. Its sequence comprises two von Willebrand factor type A-like repeats. In order to characterize the structure and domain architecture of PTMP1, recombinant protein was crystallized by vapour diffusion. The obtained crystals diffracted to 1.95 Å resolution and belonged to space group P21, with unit-cell parameters a = 62.0, b = 62.3, c = 122.6 Å, β = 102.2°. The Matthews coefficient suggested the presence of two monomers in the asymmetric unit and 48.3% solvent content.