Open AccessCrystallization and preliminary X‐ray analysis of human endothelin
Author(s) -
Waller D.,
Cudney R.,
Wolff M.,
Day J.,
Greenwood A.,
Larson S.,
McPherson A.
Publication year - 1992
Publication title -
acta crystallographica section b
Language(s) - English
Resource type - Journals
eISSN - 1600-5740
pISSN - 0108-7681
DOI - 10.1107/s0108768191010625
Subject(s) - crystallization , crystallography , diffraction , resolution (logic) , solvent , crystal (programming language) , materials science , x ray crystallography , diffusion , chemistry , optics , organic chemistry , physics , thermodynamics , artificial intelligence , computer science , programming language
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.