Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex
Crystallization of contaminating proteins is a frequently encountered problem for macromolecular crystallographers. In this study, an attempt was made to obtain a binary cocrystal structure of the SH3 domain of cortactin and a 17‐residue peptide from the Arg nonreceptor tyrosine kinase encompassing...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2012-02, Vol.68 (2), p.154-158 |
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| container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
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| creator | Liu, Weizhi MacGrath, Stacey M. Koleske, Anthony J. Boggon, Titus J. |
| description | Crystallization of contaminating proteins is a frequently encountered problem for macromolecular crystallographers. In this study, an attempt was made to obtain a binary cocrystal structure of the SH3 domain of cortactin and a 17‐residue peptide from the Arg nonreceptor tyrosine kinase encompassing a PxxPxxPxxP (PxxP1) motif. However, cocrystals could only be obtained in the presence of trace amounts of a contaminating protein. A structure solution obtained by molecular replacement followed by ARP/wARP automatic model building allowed a `sequence‐by‐crystallography' approach to discover that the contaminating protein was lysozyme. This 1.65 Å resolution crystal structure determination of a 1:1:1 heterotrimeric complex of Arg, cortactin and lysozyme thus provides an unusual `caveat emptor' warning of the dangers that underpurified proteins harbor for macromolecular crystallographers. |
| doi_str_mv | 10.1107/S1744309111056132 |
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In this study, an attempt was made to obtain a binary cocrystal structure of the SH3 domain of cortactin and a 17‐residue peptide from the Arg nonreceptor tyrosine kinase encompassing a PxxPxxPxxP (PxxP1) motif. However, cocrystals could only be obtained in the presence of trace amounts of a contaminating protein. A structure solution obtained by molecular replacement followed by ARP/wARP automatic model building allowed a `sequence‐by‐crystallography' approach to discover that the contaminating protein was lysozyme. This 1.65 Å resolution crystal structure determination of a 1:1:1 heterotrimeric complex of Arg, cortactin and lysozyme thus provides an unusual `caveat emptor' warning of the dangers that underpurified proteins harbor for macromolecular crystallographers.</description><identifier>ISSN: 1744-3091</identifier><identifier>EISSN: 1744-3091</identifier><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S1744309111056132</identifier><identifier>PMID: 22297987</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Animals ; Arg ; Arginine - chemistry ; Contamination ; cortactin ; Cortactin - chemistry ; Cortactin - metabolism ; Crystal structure ; Crystallization ; Crystallography ; Crystallography, X-Ray ; cytoskeleton ; Kinases ; Lysozyme ; Mice ; Models, Molecular ; Molecular structure ; Muramidase - chemistry ; Muramidase - isolation & purification ; Muramidase - metabolism ; Protein Binding ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; protein-protein complexes ; Proteins ; Structural Communications</subject><ispartof>Acta crystallographica. Section F, Structural biology and crystallization communications, 2012-02, Vol.68 (2), p.154-158</ispartof><rights>International Union of Crystallography, 2012</rights><rights>International Union of Crystallography 2012 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5741-dfd5c5cae645456412af6fdb223379075d44a5f681a3ba849b53575a9a50ec7c3</citedby><cites>FETCH-LOGICAL-c5741-dfd5c5cae645456412af6fdb223379075d44a5f681a3ba849b53575a9a50ec7c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3274391/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3274391/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,729,782,786,887,1419,27931,27932,45581,45582,53798,53800</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22297987$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1069477$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Weizhi</creatorcontrib><creatorcontrib>MacGrath, Stacey M.</creatorcontrib><creatorcontrib>Koleske, Anthony J.</creatorcontrib><creatorcontrib>Boggon, Titus J.</creatorcontrib><creatorcontrib>BROOKHAVEN NATIONAL LABORATORY (BNL)</creatorcontrib><title>Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex</title><title>Acta crystallographica. Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>Crystallization of contaminating proteins is a frequently encountered problem for macromolecular crystallographers. In this study, an attempt was made to obtain a binary cocrystal structure of the SH3 domain of cortactin and a 17‐residue peptide from the Arg nonreceptor tyrosine kinase encompassing a PxxPxxPxxP (PxxP1) motif. However, cocrystals could only be obtained in the presence of trace amounts of a contaminating protein. A structure solution obtained by molecular replacement followed by ARP/wARP automatic model building allowed a `sequence‐by‐crystallography' approach to discover that the contaminating protein was lysozyme. This 1.65 Å resolution crystal structure determination of a 1:1:1 heterotrimeric complex of Arg, cortactin and lysozyme thus provides an unusual `caveat emptor' warning of the dangers that underpurified proteins harbor for macromolecular crystallographers.</description><subject>Animals</subject><subject>Arg</subject><subject>Arginine - chemistry</subject><subject>Contamination</subject><subject>cortactin</subject><subject>Cortactin - chemistry</subject><subject>Cortactin - metabolism</subject><subject>Crystal structure</subject><subject>Crystallization</subject><subject>Crystallography</subject><subject>Crystallography, X-Ray</subject><subject>cytoskeleton</subject><subject>Kinases</subject><subject>Lysozyme</subject><subject>Mice</subject><subject>Models, Molecular</subject><subject>Molecular structure</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - isolation & purification</subject><subject>Muramidase - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Tertiary</subject><subject>protein-protein complexes</subject><subject>Proteins</subject><subject>Structural Communications</subject><issn>1744-3091</issn><issn>1744-3091</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFks1u1DAUhSMEoqXwAGxQBAvYBOz4b7xBGio6IEWwaFHLyvI4Nx0XJx5sT9v06fEoZSggwcr2vd85to9uUTzF6DXGSLw5xoJSgiTOJ8Yxqe8V-9tSta3dv7PfKx7FeIEQIZLPHhZ7dV1LIWdiv4BmjP5m7KE0fki6t4NO1g9lp411NukEsTRhjEk7Z2-mnu9KXa4gQfAp2B6CNVkdkjbJDtU8nFful2m_dnD9uHjQaRfhye16UHw5en9y-KFqPi8-Hs6byjBBcdV2LTPMaOCUUcYprnXHu3ZZ14QIiQRrKdWs4zOsyVLPqFwywgTTUjMERhhyULydfNebZQ-tgSEF7dQ6v1KHUXlt1e-dwa7Uub9UpBaUSJwNnk8GPiarorEJzConM4BJCiMuqRAZenl7S_DfNxCT6m004JwewG-iklhKxuSMZvLVP0mMsOSESUEy-uIP9MJvwpDTUlgQzFlmeKbwRJngYwzQ7f6GkdrOhPprJrLm2d1QdoqfQ5ABOQFX1sH4f0c1_3pUvztlFG0DqyatjQmud1odvikuiGDq9NNCnZ00x4vFGVYN-QFvq9L-</recordid><startdate>201202</startdate><enddate>201202</enddate><creator>Liu, Weizhi</creator><creator>MacGrath, Stacey M.</creator><creator>Koleske, Anthony J.</creator><creator>Boggon, Titus J.</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</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>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>7U5</scope><scope>L7M</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>201202</creationdate><title>Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex</title><author>Liu, Weizhi ; MacGrath, Stacey M. ; Koleske, Anthony J. ; Boggon, Titus J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5741-dfd5c5cae645456412af6fdb223379075d44a5f681a3ba849b53575a9a50ec7c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animals</topic><topic>Arg</topic><topic>Arginine - chemistry</topic><topic>Contamination</topic><topic>cortactin</topic><topic>Cortactin - chemistry</topic><topic>Cortactin - metabolism</topic><topic>Crystal structure</topic><topic>Crystallization</topic><topic>Crystallography</topic><topic>Crystallography, X-Ray</topic><topic>cytoskeleton</topic><topic>Kinases</topic><topic>Lysozyme</topic><topic>Mice</topic><topic>Models, Molecular</topic><topic>Molecular structure</topic><topic>Muramidase - chemistry</topic><topic>Muramidase - isolation & purification</topic><topic>Muramidase - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, Tertiary</topic><topic>protein-protein complexes</topic><topic>Proteins</topic><topic>Structural Communications</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Weizhi</creatorcontrib><creatorcontrib>MacGrath, Stacey M.</creatorcontrib><creatorcontrib>Koleske, Anthony J.</creatorcontrib><creatorcontrib>Boggon, Titus J.</creatorcontrib><creatorcontrib>BROOKHAVEN NATIONAL LABORATORY (BNL)</creatorcontrib><collection>Istex</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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. 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F</addtitle><date>2012-02</date><risdate>2012</risdate><volume>68</volume><issue>2</issue><spage>154</spage><epage>158</epage><pages>154-158</pages><issn>1744-3091</issn><eissn>1744-3091</eissn><eissn>2053-230X</eissn><abstract>Crystallization of contaminating proteins is a frequently encountered problem for macromolecular crystallographers. In this study, an attempt was made to obtain a binary cocrystal structure of the SH3 domain of cortactin and a 17‐residue peptide from the Arg nonreceptor tyrosine kinase encompassing a PxxPxxPxxP (PxxP1) motif. However, cocrystals could only be obtained in the presence of trace amounts of a contaminating protein. A structure solution obtained by molecular replacement followed by ARP/wARP automatic model building allowed a `sequence‐by‐crystallography' approach to discover that the contaminating protein was lysozyme. 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| subjects | Animals Arg Arginine - chemistry Contamination cortactin Cortactin - chemistry Cortactin - metabolism Crystal structure Crystallization Crystallography Crystallography, X-Ray cytoskeleton Kinases Lysozyme Mice Models, Molecular Molecular structure Muramidase - chemistry Muramidase - isolation & purification Muramidase - metabolism Protein Binding Protein Structure, Quaternary Protein Structure, Tertiary protein-protein complexes Proteins Structural Communications |
| title | Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex |
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