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Highly ordered crystals of the plant seed protein crambin.
Authors:M M Teeter  W A Hendrickson
Institution:Department of Chemistry Boston University 685 Commonwealth Avenue Boston, Ma. 02215, U.S.A.;Laboratory for the Structure of Matter Naval Research Laboratory Washington D.C. 20375, U.S.A.
Abstract:Crystals of crambin, a plant seed protein of molecular weight 5000, diffract X-rays strongly to the interplanar spacing limit of 0.88 Å. These diffraction data should allow a definition of atomic structure that is on a par with that typically obtained from crystals of small organic molecules. The crystals are in space group P21 and have unit cell dimensions a = 41.1 A?, b = 18.7 A?, c = 22·7 A?, and β = 90.6 °. The asymmetric unit contains one protein molecule.
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