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dc.contributor.authorBrünger, Axel T.
dc.date.accessioned2023-11-03T08:57:18Z
dc.date.available2023-11-03T08:57:18Z
dc.date.issued1988
dc.date.submitted2023-11-03
dc.identifier.citationAdvances in protein design, 35 - 37en_US
dc.identifier.isbn3527280243
dc.identifier.isbn0895739534
dc.identifier.issn0930-4320
dc.identifier.urihttp://hdl.handle.net/10033/623517
dc.description.abstractConventional refinementof biological macromolecules involvesa series of steps, each of which consists ofa few cyclesofrestrained least-squares refinement with stereochemical and internal packingconstraints orrestraints that are followed by rebuilding the modelstructure with interactive computer graphics. Duringthefinal stages of refinement solvent molecules are usually included and alternative conformations for some atomsor residues in the protein may be introduced.en_US
dc.language.isoenen_US
dc.publisherGBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweigen_US
dc.relation.ispartofseriesGBF monographs ; Volume 12en_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleA ComputationalTool for Structural Biology: Crystallographic Refinement by Simulated Annealingen_US
dc.typeBook chapteren_US
dc.typeconference paperen_US
dc.contributor.departmentThe Howard Hughes MedicalInstitute and Department of Molecular Biophysics and Biochemistry, Yale Universit, New Haven, CT 06511en_US
dc.identifier.journalAdvances in protein design, 1988en_US
refterms.dateFOA2023-11-03T08:57:19Z


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