Crystallization and preliminary X-ray analysis of the C-type lectin domain of the spicule matrix protein SM50 from Strongylocentrotus purpuratus

Kurzanzeige
dc.contributor.authorJuneja, Puneet
dc.contributor.authorRao, Ashit
dc.contributor.authorCölfen, Helmut
dc.contributor.authorDiederichs, Kay
dc.contributor.authorWelte, Wolfram
dc.date.accessioned2014-08-04T06:58:20Zdeu
dc.date.available2014-08-04T06:58:20Zdeu
dc.date.issued2014-02
dc.description.abstractSea 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.eng
dc.description.versionpublished
dc.identifier.citationActa Crystallographica / Section F ; 70 (2014), 2. - S. 260-262deu
dc.identifier.doi10.1107/S2053230X14000880deu
dc.identifier.pmid24637770
dc.identifier.ppn417241208
dc.identifier.urihttp://kops.uni-konstanz.de/handle/123456789/28622
dc.language.isoengdeu
dc.legacy.dateIssued2014-08-04deu
dc.rightsterms-of-usedeu
dc.rights.urihttps://rightsstatements.org/page/InC/1.0/deu
dc.subjectC-type lectinsdeu
dc.subjectSM50deu
dc.subjectspiculogenesisdeu
dc.subjectStrongylocentrotus purpuratusdeu
dc.subject.ddc540deu
dc.titleCrystallization and preliminary X-ray analysis of the C-type lectin domain of the spicule matrix protein SM50 from Strongylocentrotus purpuratuseng
dc.typeJOURNAL_ARTICLEdeu
dspace.entity.typePublication
kops.citation.bibtex
@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}
}
kops.citation.iso690JUNEJA, 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/S2053230X14000880deu
kops.citation.iso690JUNEJA, 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/S2053230X14000880eng
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kops.description.commentCorrigendum: https://doi.org/10.1107/S2053230X22007853
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kops.sourcefield.plainActa Crystallographica Section F Structural Biology Communications. 2014, 70(2), pp. 260-262. eISSN 2053-230X. Available under: doi: 10.1107/S2053230X14000880eng
kops.submitter.emailoleg.kozlov@uni-konstanz.dedeu
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