Protein structure is only as good as the data [electronic resource].
- Upton, N.Y. : Brookhaven National Laboratory, 1984. and Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy.
- Physical Description:
- Pages: 19 : digital, PDF file
- Additional Creators:
- Brookhaven National Laboratory and United States. Department of Energy. Office of Scientific and Technical Information
- Restrictions on Access:
- Free-to-read Unrestricted online access
- Careful selection of the best diffraction geometry matched to the sample, with use of high resolution two-dimensional detectors and a mask integration procedure will allow the collection of statistically accurate data for many proteins and crystals with a sample size of at least 1 mm/sup 3/. Accurate data and improved refinement techniques will allow the determination of all atoms including hydrogens, hydrogen-deuterium exchange, water of hydration, and solvent water densities. The developments in the above described neutron techniques have been gradually used in the analysis of myoglobins, gramicidin, trypsin, and crambin. 16 references, 11 figures, 2 tables.
- Published through SciTech Connect., 06/01/1984., "bnl-34679", " conf-8206240-8", "DE84012904", Brookhaven symposium biology 32, Upton, NY, USA, 1 Jun 1982., and Schoenborn, B.P.
- Funding Information:
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