ArticleActa crystallographica. Section F, Structural biology communications2014
Crystallization and preliminary X-ray diffraction analysis of proximal thread matrix protein 1 (PTMP1) from Mytilus galloprovincialis.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Insights into the Red SeaweedPlants (Basel, Switzerland) · 2025Article
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4 authors.
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Abstract
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.
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