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Purification, crystallization and preliminary crystallographic analysis of very-long-chain acyl-­CoA dehydrogenase from Caenorhabditis elegans

Authors
Journal
Acta Crystallographica Section F Structural Biology and Crystallization Communications
1744-3091
Publisher
International Union of Crystallography
Publication Date
Volume
66
Issue
4
Identifiers
DOI: 10.1107/s1744309110005002
Keywords
  • Crystallization Communications
Disciplines
  • Biology

Abstract

Very-long-chain acyl-CoA dehydrogenase from Caenorhabditis elegans (cVLCAD) has been crystallized in space group C2 and its X-ray diffraction data set has been collected to 1.6 Å resolution. Unlike other VLCADs that were reported to form dimers, the purified cVLCAD was found as a homotetrameric protein according to static light-scattering measurements.

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