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    Acta Crystallogr B. 1992 Apr 1;48 ( Pt 2):239-40.

    Crystallization and preliminary X-ray analysis of human endothelin.

    Wolff M, Day J, Greenwood A, Larson S, McPherson A.

    Source

    Department of Biochemistry, University of California, Riverside 92521.

    Abstract

    Endothelin, a potent regulator of vasoconstriction and hypertension, is a naturally produced peptide of 21 amino acids containing two disulfide bonds. We have crystallized endothelin from humans using the vapor-diffusion technique, characterized the crystals by X-ray diffraction analysis, and have collected the X-ray intensities to a resolution of 1.8 A. The crystals, which demonstrate physical properties similar to most protein crystals and have a comparable solvent content, are hexagonal prisms that frequently grow to lengths of 400 microns and widths of 150 microns. The space group of the crystals is P6(1)22 (or P6(5)22), with a = 27.4, c = 79.6 A. There is one molecule of endothelin in the asymmetric unit of the crystals.

    PMID:
    1515112
    [PubMed - indexed for MEDLINE]

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