Publikation: Crystallization and preliminary X-ray analysis of the C-type lectin domain of the spicule matrix protein SM50 from Strongylocentrotus purpuratus
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2014
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Acta Crystallographica Section F Structural Biology Communications. 2014, 70(2), pp. 260-262. eISSN 2053-230X. Available under: doi: 10.1107/S2053230X14000880
Zusammenfassung
Sea urchin spicules have a calcitic mesocrystalline architecture that is closely associated with a matrix of proteins and amorphous minerals. The mechanism underlying spicule formation involves complex processes encompassing spatio-temporally regulated organic–inorganic interactions. C-type lectin domains are present in several spicule matrix proteins in Strongylocentrotus purpuratus, implying their role in spiculogenesis. In this study, the C-type lectin domain of SM50 was overexpressed, purified and crystallized using a vapour-diffusion method. The crystal diffracted to a resolution of 2.85 Å and belonged to space group P212121, with unit-cell parameters a = 100.6, b = 115.4, c = 130.6 Å, α = β = γ = 90°. Assuming 50% solvent content, six chains are expected to be present in the asymmetric unit.
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540 Chemie
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C-type lectins, SM50, spiculogenesis, Strongylocentrotus purpuratus
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JUNEJA, Puneet, Ashit RAO, Helmut CÖLFEN, Kay DIEDERICHS, Wolfram WELTE, 2014. Crystallization and preliminary X-ray analysis of the C-type lectin domain of the spicule matrix protein SM50 from Strongylocentrotus purpuratus. In: Acta Crystallographica Section F Structural Biology Communications. 2014, 70(2), pp. 260-262. eISSN 2053-230X. Available under: doi: 10.1107/S2053230X14000880BibTex
@article{Juneja2014-02Cryst-28622,
year={2014},
doi={10.1107/S2053230X14000880},
title={Crystallization and preliminary X-ray analysis of the C-type lectin domain of the spicule matrix protein SM50 from Strongylocentrotus purpuratus},
number={2},
volume={70},
journal={Acta Crystallographica Section F Structural Biology Communications},
pages={260--262},
author={Juneja, Puneet and Rao, Ashit and Cölfen, Helmut and Diederichs, Kay and Welte, Wolfram},
note={Corrigendum: https://doi.org/10.1107/S2053230X22007853}
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<dcterms:abstract xml:lang="eng">Sea urchin spicules have a calcitic mesocrystalline architecture that is closely associated with a matrix of proteins and amorphous minerals. The mechanism underlying spicule formation involves complex processes encompassing spatio-temporally regulated organic–inorganic interactions. C-type lectin domains are present in several spicule matrix proteins in Strongylocentrotus purpuratus, implying their role in spiculogenesis. In this study, the C-type lectin domain of SM50 was overexpressed, purified and crystallized using a vapour-diffusion method. The crystal diffracted to a resolution of 2.85 Å and belonged to space group P2<sub>1</sub>2<sub>1</sub>2<sub>1</sub>, with unit-cell parameters a = 100.6, b = 115.4, c = 130.6 Å, α = β = γ = 90°. Assuming 50% solvent content, six chains are expected to be present in the asymmetric unit.</dcterms:abstract>
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Corrigendum: https://doi.org/10.1107/S2053230X22007853
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