Crystallization of a synthetic analog of calcium-binding site III of rabbit skeletal troponin C
Single crystals of the calcium-binding peptide AcA98STnC (90–123)amide, which is a synthetic fragment analog of rabbit skeletal troponin C calcium-binding site III, have been grown in the tetragonal crystal system. Crystals were developed to a maximum size of 0.60 × 0.60 × 0.75-mm by the technique o...
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Veröffentlicht in: | The Journal of biological chemistry 1989-06, Vol.264 (17), p.10261-10263 |
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container_title | The Journal of biological chemistry |
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creator | Delbaere, L T J Vandonselaar, M Reid, R E |
description | Single crystals of the calcium-binding peptide AcA98STnC (90–123)amide, which is a synthetic fragment analog of rabbit skeletal troponin C calcium-binding site III, have been grown in the tetragonal crystal system. Crystals were developed to a maximum size of 0.60 × 0.60 × 0.75-mm by the technique of washing and reseeding. The space group is I41 with a = 40.21(1) Å, c = 34.07(1) Å; there is 1 polypeptide fragment/crystallographic asymmetric unit, and the solvent content is estimated to be 29%. The crystals diffract to at least 1.8-Å d spacings and are stable in the x-ray beam for 1 week. |
doi_str_mv | 10.1016/S0021-9258(18)81793-8 |
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Crystals were developed to a maximum size of 0.60 × 0.60 × 0.75-mm by the technique of washing and reseeding. The space group is I41 with a = 40.21(1) Å, c = 34.07(1) Å; there is 1 polypeptide fragment/crystallographic asymmetric unit, and the solvent content is estimated to be 29%. The crystals diffract to at least 1.8-Å d spacings and are stable in the x-ray beam for 1 week.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)81793-8</identifier><identifier>PMID: 2722867</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Binding and carrier proteins ; Binding Sites ; Biological and medical sciences ; Calcium - metabolism ; Crystallization ; Fundamental and applied biological sciences. 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Crystals were developed to a maximum size of 0.60 × 0.60 × 0.75-mm by the technique of washing and reseeding. The space group is I41 with a = 40.21(1) Å, c = 34.07(1) Å; there is 1 polypeptide fragment/crystallographic asymmetric unit, and the solvent content is estimated to be 29%. The crystals diffract to at least 1.8-Å d spacings and are stable in the x-ray beam for 1 week.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding and carrier proteins</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Calcium - metabolism</subject><subject>Crystallization</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Muscles - metabolism</topic><topic>Peptides - isolation & purification</topic><topic>Peptides - metabolism</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>skeletal muscle</topic><topic>Troponin - metabolism</topic><topic>Troponin C</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Delbaere, L T J</creatorcontrib><creatorcontrib>Vandonselaar, M</creatorcontrib><creatorcontrib>Reid, R E</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Delbaere, L T J</au><au>Vandonselaar, M</au><au>Reid, R E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization of a synthetic analog of calcium-binding site III of rabbit skeletal troponin C</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1989-06-15</date><risdate>1989</risdate><volume>264</volume><issue>17</issue><spage>10261</spage><epage>10263</epage><pages>10261-10263</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Single crystals of the calcium-binding peptide AcA98STnC (90–123)amide, which is a synthetic fragment analog of rabbit skeletal troponin C calcium-binding site III, have been grown in the tetragonal crystal system. Crystals were developed to a maximum size of 0.60 × 0.60 × 0.75-mm by the technique of washing and reseeding. The space group is I41 with a = 40.21(1) Å, c = 34.07(1) Å; there is 1 polypeptide fragment/crystallographic asymmetric unit, and the solvent content is estimated to be 29%. The crystals diffract to at least 1.8-Å d spacings and are stable in the x-ray beam for 1 week.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2722867</pmid><doi>10.1016/S0021-9258(18)81793-8</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Analytical, structural and metabolic biochemistry Animals Binding and carrier proteins Binding Sites Biological and medical sciences Calcium - metabolism Crystallization Fundamental and applied biological sciences. Psychology Muscles - metabolism Peptides - isolation & purification Peptides - metabolism Protein Binding Protein Conformation Proteins Rabbits skeletal muscle Troponin - metabolism Troponin C X-Ray Diffraction |
title | Crystallization of a synthetic analog of calcium-binding site III of rabbit skeletal troponin C |
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