David Waller - Crystallization and preliminary X-ray analysis of human endothelin

Document created by David Waller on Aug 22, 2014
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  Publication Details (including relevant citation   information):

  Acta Cryst. (1992). B48, 239-240


  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 Angstroms. 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   micrometers and widths of 150 micrometers. The space group of the   crystals is P6,22 (or P6,22), with a=27.4,   c=79.6 Angstroms. There is one molecule of endothelin in the   asymmetric unit of crystals.

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