Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule
A hybrid molecule consisting of calmodulin (CaM) and the CaM‐binding domain of olfactory nucleotide‐gated ion‐channel peptide (CaM‐OLFp) was purified and crystallized by the hanging‐drop vapour‐diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 Å at cryogenic temperat...
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Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-08, Vol.61 (8), p.785-787 |
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Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | A hybrid molecule consisting of calmodulin (CaM) and the CaM‐binding domain of olfactory nucleotide‐gated ion‐channel peptide (CaM‐OLFp) was purified and crystallized by the hanging‐drop vapour‐diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 Å at cryogenic temperature (100 K) using X‐rays from a rotating anode (Cu, wavelength 1.54 Å). The crystal belongs to the monoclinic space group C2, with unit‐cell parameters a = 64.76, b = 36.23, c = 70.96 Å, α = γ = 90, β = 109.4°. Analysis of the packing density shows that the asymmetric unit contains one CaM‐OLFp hybrid molecule with a solvent content of 36.42%. |
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ISSN: | 1744-3091 1744-3091 |
DOI: | 10.1107/S1744309105023006 |