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Crystallization and preliminary X‐ray diffraction analysis of proximal thread matrix protein 1 (PTMP1) from Mytilus galloprovincialis
Author(s) -
Suhre Michael H.,
Scheibel Thomas,
Steegborn Clemens,
Gertz Melanie
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14006165
Subject(s) - thread (computing) , crystallization , monomer , mytilus , crystallography , diffraction , chemistry , materials science , polymer , biology , optics , physics , fishery , computer science , organic chemistry , operating system
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 P 2 1 , 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.