{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/22013"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/22013","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Diffuse X-ray scattering from tropomyosin crystals","abstract":"Motions in proteins are often an important part of their function. Structural information about the protein is hence incomplete without an understanding of the protein dynamics. X-ray crystallography is the technique used in the majority of protein structure determinations; from a crystallographic standpoint as well, the movement of the molecules in the crystal which profoundly affect the X-ray scattering are important. All motions in the crystal affect the Bragg scattering and also give rise to diffuse scattering between and surrounding the Bragg spots. The diffuse X-ray scattering may comprise a large part of the total scattering from the crystal, and it contains information about the correlation of motions that is not available from analysis of the Bragg diffraction peaks.","abstract_html":"Motions in proteins are often an important part of their function. Structural information about the protein is hence incomplete without an understanding of the protein dynamics. X-ray crystallography is the technique used in the majority of protein structure determinations; from a crystallographic standpoint as well, the movement of the molecules in the crystal which profoundly affect the X-ray scattering are important. All motions in the crystal affect the Bragg scattering and also give rise to diffuse scattering between and surrounding the Bragg spots. The diffuse X-ray scattering may comprise a large part of the total scattering from the crystal, and it contains information about the correlation of motions that is not available from analysis of the Bragg diffraction peaks.","abstract_has_math":false,"creators":["Chacko, Susan"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biophysics","degree_department":null,"school":null,"contributors":["Phillips, George N., Jr.,"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T13:26:11Z","date_published":"2011-05-07T13:26:11Z","updated_at":"2026-07-22T22:25:19Z","subjects":["Biophysics, General"],"languages":["eng"],"rights":["Copyright 1991 Chacko, Susan"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9136564","(UMI)AAI9136564"],"render_values":[{"text":"AAI9136564","href":null,"code":true},{"text":"(UMI)AAI9136564","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/22013","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Phillips, George N., Jr.,"]},{"key":"dc:creator","label":"Author","values":["Chacko, Susan"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T13:26:11Z","10000-01-01","1991"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biophysics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biophysics, General"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1991 Chacko, Susan"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9136564","(UMI)AAI9136564","http://hdl.handle.net/2142/22013"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Motions in proteins are often an important part of their function. Structural information about the protein is hence incomplete without an understanding of the protein dynamics. X-ray crystallography is the technique used in the majority of protein structure determinations; from a crystallographic standpoint as well, the movement of the molecules in the crystal which profoundly affect the X-ray scattering are important. All motions in the crystal affect the Bragg scattering and also give rise to diffuse scattering between and surrounding the Bragg spots. The diffuse X-ray scattering may comprise a large part of the total scattering from the crystal, and it contains information about the correlation of motions that is not available from analysis of the Bragg diffraction peaks.","Tropomyosin is a muscle protein that is involved in control of the muscle contraction process. Changes in the structural conformation of the protein are an essential part of this process. Tropomyosin crystals exhibit striking diffuse scattering patterns which are related to its inherent flexibility and motions in the crystal. Diffuse scattering data along all the major directions of the crystal have been measured. A complete three-dimensional diffuse scattering data set has been simulated, and this has been compared to the experimental data in the measured directions. A combination of empirical and analytical methods were used to perform the simulations, and the amplitudes, directions and correlation distances of the motions within the crystal have been calculated.","Made available in DSpace on 2011-05-07T13:26:11Z (GMT). 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Structural information about the protein is hence incomplete without an understanding of the protein dynamics. X-ray crystallography is the technique used in the majority of protein structure determinations; from a crystallographic standpoint as well, the movement of the molecules in the crystal which profoundly affect the X-ray scattering are important. All motions in the crystal affect the Bragg scattering and also give rise to diffuse scattering between and surrounding the Bragg spots. The diffuse X-ray scattering may comprise a large part of the total scattering from the crystal, and it contains information about the correlation of motions that is not available from analysis of the Bragg diffraction peaks.","Tropomyosin is a muscle protein that is involved in control of the muscle contraction process. Changes in the structural conformation of the protein are an essential part of this process. Tropomyosin crystals exhibit striking diffuse scattering patterns which are related to its inherent flexibility and motions in the crystal. Diffuse scattering data along all the major directions of the crystal have been measured. A complete three-dimensional diffuse scattering data set has been simulated, and this has been compared to the experimental data in the measured directions. A combination of empirical and analytical methods were used to perform the simulations, and the amplitudes, directions and correlation distances of the motions within the crystal have been calculated.","Made available in DSpace on 2011-05-07T13:26:11Z (GMT). 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