Structural studies of tropomyosin by cryoelectron microscopy and x-ray diffraction
A comparison has been made between cryoelectron microscope images and the x-ray structure of one projection of the Bailey tropomyosin crystal. The computed transforms of the electron micrographs extend to a resolution of approximately 18 A compared with the reflections from x-ray crystallography whi...
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Veröffentlicht in: | Biophysical journal 1991-04, Vol.59 (4), p.805-814 |
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creator | Cabral-Lilly, D. Phillips, G.N. Sosinsky, G.E. Melanson, L. Chacko, S. Cohen, C. |
description | A comparison has been made between cryoelectron microscope images and the x-ray structure of one projection of the Bailey tropomyosin crystal. The computed transforms of the electron micrographs extend to a resolution of approximately 18 A compared with the reflections from x-ray crystallography which extend to 15 A. After correction of the images for lattice distortions and the contrast transfer function, the structure factors were constrained to the plane group (pmg) symmetry of this projection. Amplitude and phase data for five images were compared with the corresponding view from the three-dimensional x-ray diffraction data (Phillips, G.N., Jr., J.P. Fillers, and C. Cohen. 1986. J. Mol. Biol. 192: 111–131). The average R factor between the electron microscopy and x-ray amplitudes was 15%, with an amplitude-weighted mean phase difference of 4.8 degrees. The density maps derived from cryoelectron microscopy contain structural features similar to those from x-ray diffraction: these include the width and run of the filaments and their woven appearance at the crossover regions. Preliminary images obtained from frozen-hydrated tropomyosin/troponin cocrystals suggest that this approach may provide structural details not readily obtainable from x-ray diffraction studies. |
doi_str_mv | 10.1016/S0006-3495(91)82293-7 |
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The computed transforms of the electron micrographs extend to a resolution of approximately 18 A compared with the reflections from x-ray crystallography which extend to 15 A. After correction of the images for lattice distortions and the contrast transfer function, the structure factors were constrained to the plane group (pmg) symmetry of this projection. Amplitude and phase data for five images were compared with the corresponding view from the three-dimensional x-ray diffraction data (Phillips, G.N., Jr., J.P. Fillers, and C. Cohen. 1986. J. Mol. Biol. 192: 111–131). The average R factor between the electron microscopy and x-ray amplitudes was 15%, with an amplitude-weighted mean phase difference of 4.8 degrees. The density maps derived from cryoelectron microscopy contain structural features similar to those from x-ray diffraction: these include the width and run of the filaments and their woven appearance at the crossover regions. Preliminary images obtained from frozen-hydrated tropomyosin/troponin cocrystals suggest that this approach may provide structural details not readily obtainable from x-ray diffraction studies.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(91)82293-7</identifier><identifier>PMID: 2065187</identifier><identifier>CODEN: BIOJAU</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Animals ; Biological and medical sciences ; Freezing ; Fundamental and applied biological sciences. 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The computed transforms of the electron micrographs extend to a resolution of approximately 18 A compared with the reflections from x-ray crystallography which extend to 15 A. After correction of the images for lattice distortions and the contrast transfer function, the structure factors were constrained to the plane group (pmg) symmetry of this projection. Amplitude and phase data for five images were compared with the corresponding view from the three-dimensional x-ray diffraction data (Phillips, G.N., Jr., J.P. Fillers, and C. Cohen. 1986. J. Mol. Biol. 192: 111–131). The average R factor between the electron microscopy and x-ray amplitudes was 15%, with an amplitude-weighted mean phase difference of 4.8 degrees. The density maps derived from cryoelectron microscopy contain structural features similar to those from x-ray diffraction: these include the width and run of the filaments and their woven appearance at the crossover regions. Preliminary images obtained from frozen-hydrated tropomyosin/troponin cocrystals suggest that this approach may provide structural details not readily obtainable from x-ray diffraction studies.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Freezing</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Microscopy, Electron - methods</subject><subject>Molecular biophysics</subject><subject>Myocardium</subject><subject>Rabbits</subject><subject>Tropomyosin - chemistry</subject><subject>Tropomyosin - ultrastructure</subject><subject>Troponin - chemistry</subject><subject>Troponin - ultrastructure</subject><subject>X-Ray Diffraction - methods</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV9rFTEQxYMo9bb6EQr7IKIPa5NsNn9eFClWhUKh1eeQTSYa2U2uyW5xv31zey8XffIpMOc3k5lzEDon-B3BhF_cYYx52zHVv1HkraRUda14gjakZ7TFWPKnaHNEnqPTUn5hTGiPyQk6oZj3RIoNur2b82LnJZuxKfPiApQm-WbOaZumNZUQm2FtbF4TjGBrOTZTsDkVm7ZrY6Jr_rTZrI0L3mdj55DiC_TMm7HAy8N7hr5fffp2-aW9vvn89fLjdWuZInM7OOV9x4xkvvOGdU7YYfDCUeUkV4A9FgAglRS96Ln0xksnFAVSRUmZ687Q-_3c7TJM4CzEuV6htzlMJq86maD_VWL4qX-ke02oJJTxOuD1YUBOvxcos55CsTCOJkJaipaYc4oVrmC_B3eHlwz--AnBeheGfgxD75zWiujHMLSofed_b3jsOrhf9VcH3RRrxmpgtKEcsZ4KRhSt2Ic9BtXN-wBZFxsgWnAh10y0S-E_izwADeSpjQ</recordid><startdate>19910401</startdate><enddate>19910401</enddate><creator>Cabral-Lilly, D.</creator><creator>Phillips, G.N.</creator><creator>Sosinsky, G.E.</creator><creator>Melanson, L.</creator><creator>Chacko, S.</creator><creator>Cohen, C.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19910401</creationdate><title>Structural studies of tropomyosin by cryoelectron microscopy and x-ray diffraction</title><author>Cabral-Lilly, D. ; Phillips, G.N. ; Sosinsky, G.E. ; Melanson, L. ; Chacko, S. ; Cohen, C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c491t-bd9ff34a84f3fa43d7cbbf7d29d869e0f07eee898757568faf8d792e169e824d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Freezing</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Microscopy, Electron - methods</topic><topic>Molecular biophysics</topic><topic>Myocardium</topic><topic>Rabbits</topic><topic>Tropomyosin - chemistry</topic><topic>Tropomyosin - ultrastructure</topic><topic>Troponin - chemistry</topic><topic>Troponin - ultrastructure</topic><topic>X-Ray Diffraction - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cabral-Lilly, D.</creatorcontrib><creatorcontrib>Phillips, G.N.</creatorcontrib><creatorcontrib>Sosinsky, G.E.</creatorcontrib><creatorcontrib>Melanson, L.</creatorcontrib><creatorcontrib>Chacko, S.</creatorcontrib><creatorcontrib>Cohen, C.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cabral-Lilly, D.</au><au>Phillips, G.N.</au><au>Sosinsky, G.E.</au><au>Melanson, L.</au><au>Chacko, S.</au><au>Cohen, C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural studies of tropomyosin by cryoelectron microscopy and x-ray diffraction</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1991-04-01</date><risdate>1991</risdate><volume>59</volume><issue>4</issue><spage>805</spage><epage>814</epage><pages>805-814</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><coden>BIOJAU</coden><abstract>A comparison has been made between cryoelectron microscope images and the x-ray structure of one projection of the Bailey tropomyosin crystal. The computed transforms of the electron micrographs extend to a resolution of approximately 18 A compared with the reflections from x-ray crystallography which extend to 15 A. After correction of the images for lattice distortions and the contrast transfer function, the structure factors were constrained to the plane group (pmg) symmetry of this projection. Amplitude and phase data for five images were compared with the corresponding view from the three-dimensional x-ray diffraction data (Phillips, G.N., Jr., J.P. Fillers, and C. Cohen. 1986. J. Mol. Biol. 192: 111–131). The average R factor between the electron microscopy and x-ray amplitudes was 15%, with an amplitude-weighted mean phase difference of 4.8 degrees. The density maps derived from cryoelectron microscopy contain structural features similar to those from x-ray diffraction: these include the width and run of the filaments and their woven appearance at the crossover regions. Preliminary images obtained from frozen-hydrated tropomyosin/troponin cocrystals suggest that this approach may provide structural details not readily obtainable from x-ray diffraction studies.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2065187</pmid><doi>10.1016/S0006-3495(91)82293-7</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Biological and medical sciences Freezing Fundamental and applied biological sciences. Psychology Microscopy, Electron - methods Molecular biophysics Myocardium Rabbits Tropomyosin - chemistry Tropomyosin - ultrastructure Troponin - chemistry Troponin - ultrastructure X-Ray Diffraction - methods |
title | Structural studies of tropomyosin by cryoelectron microscopy and x-ray diffraction |
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