Cryo-EM Structure of Bovine Chaperonin TRiC/CCT in Open Conformation
In this work, conditions were selected for obtaining a sample of eukaryotic chaperonin TRiC suitable for studying by cryo-electron microscopy. Using the method of differential scanning (time-resolved) fluorimetry, the temperature stability of protein samples at different concentrations of salt and g...
Gespeichert in:
| Veröffentlicht in: | Moscow University biological sciences bulletin 2023-12, Vol.78 (Suppl 1), p.S50-S55 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | S55 |
|---|---|
| container_issue | Suppl 1 |
| container_start_page | S50 |
| container_title | Moscow University biological sciences bulletin |
| container_volume | 78 |
| creator | Stanishneva-Konovalova, T. B. Pichkur, E. B. Kudryavtseva, S. S. Yaroshevich, I. A. Semenov, A. N. Maksimov, E. G. Moiseenko, A. V. Volokh, O. I. Muronets, V. I. |
| description | In this work, conditions were selected for obtaining a sample of eukaryotic chaperonin TRiC suitable for studying by cryo-electron microscopy. Using the method of differential scanning (time-resolved) fluorimetry, the temperature stability of protein samples at different concentrations of salt and glycerol was compared, and then the selected conditions were used to prepare the sample for microscopy. As a result, the structure of bovine TRiC in an open conformation was obtained at 4.42 Å resolution. |
| doi_str_mv | 10.3103/S0096392523700219 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_2955344101</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2955344101</sourcerecordid><originalsourceid>FETCH-LOGICAL-c1839-2bb5a2dfa196faccf5924edcd87cd56bb9bf6118388da1a6bb28bce6bfe986ab3</originalsourceid><addsrcrecordid>eNp1kF9LwzAUxYMoOKcfwLeAz3X507TNo8ZNhcnATfCtJGmiHS6pSSvs25tRwQfx6V7u-Z1z4QBwidE1xYjO1gjxgnLCCC0RIpgfgQnmNM9Kjl-PweQgZwf9FJzFuEWIMU75BNyJsPfZ_Amu-zDofggGegtv_VfrDBTvsjPBu9bBzXMrZkJsYNpXnXFQeGd92Mm-9e4cnFj5Ec3Fz5yCl8V8Ix6y5er-UdwsM40ryjOiFJOksRLzwkqtLeMkN41uqlI3rFCKK1vghFZVI7FMB1IpbQplDa8KqegUXI25XfCfg4l9vfVDcOllTThjNM8xwonCI6WDjzEYW3eh3cmwrzGqD2XVf8pKHjJ6YmLdmwm_yf-bvgFEPGr9</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2955344101</pqid></control><display><type>article</type><title>Cryo-EM Structure of Bovine Chaperonin TRiC/CCT in Open Conformation</title><source>SpringerLink Journals - AutoHoldings</source><creator>Stanishneva-Konovalova, T. B. ; Pichkur, E. B. ; Kudryavtseva, S. S. ; Yaroshevich, I. A. ; Semenov, A. N. ; Maksimov, E. G. ; Moiseenko, A. V. ; Volokh, O. I. ; Muronets, V. I.</creator><creatorcontrib>Stanishneva-Konovalova, T. B. ; Pichkur, E. B. ; Kudryavtseva, S. S. ; Yaroshevich, I. A. ; Semenov, A. N. ; Maksimov, E. G. ; Moiseenko, A. V. ; Volokh, O. I. ; Muronets, V. I.</creatorcontrib><description>In this work, conditions were selected for obtaining a sample of eukaryotic chaperonin TRiC suitable for studying by cryo-electron microscopy. Using the method of differential scanning (time-resolved) fluorimetry, the temperature stability of protein samples at different concentrations of salt and glycerol was compared, and then the selected conditions were used to prepare the sample for microscopy. As a result, the structure of bovine TRiC in an open conformation was obtained at 4.42 Å resolution.</description><identifier>ISSN: 0096-3925</identifier><identifier>EISSN: 1934-791X</identifier><identifier>DOI: 10.3103/S0096392523700219</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Biochemistry ; Biomedical and Life Sciences ; Cell Biology ; Electron microscopy ; Life Sciences ; Plant Sciences ; Short Communication ; Zoology</subject><ispartof>Moscow University biological sciences bulletin, 2023-12, Vol.78 (Suppl 1), p.S50-S55</ispartof><rights>Allerton Press, Inc. 2023. ISSN 0096-3925, Moscow University Biological Sciences Bulletin, 2023, Vol. 78, Suppl. 1, pp. S50–S55. © Allerton Press, Inc., 2023. Russian Text © The Author(s), 2023, published in Vestnik Moskovskogo Universiteta, Seriya 16: Biologiya, 2023, Vol. 78, No. 3 Supplement, pp. 40–46.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c1839-2bb5a2dfa196faccf5924edcd87cd56bb9bf6118388da1a6bb28bce6bfe986ab3</cites><orcidid>0000-0003-1112-2356 ; 0000-0002-8427-8178</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.3103/S0096392523700219$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.3103/S0096392523700219$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Stanishneva-Konovalova, T. B.</creatorcontrib><creatorcontrib>Pichkur, E. B.</creatorcontrib><creatorcontrib>Kudryavtseva, S. S.</creatorcontrib><creatorcontrib>Yaroshevich, I. A.</creatorcontrib><creatorcontrib>Semenov, A. N.</creatorcontrib><creatorcontrib>Maksimov, E. G.</creatorcontrib><creatorcontrib>Moiseenko, A. V.</creatorcontrib><creatorcontrib>Volokh, O. I.</creatorcontrib><creatorcontrib>Muronets, V. I.</creatorcontrib><title>Cryo-EM Structure of Bovine Chaperonin TRiC/CCT in Open Conformation</title><title>Moscow University biological sciences bulletin</title><addtitle>Moscow Univ. Biol.Sci. Bull</addtitle><description>In this work, conditions were selected for obtaining a sample of eukaryotic chaperonin TRiC suitable for studying by cryo-electron microscopy. Using the method of differential scanning (time-resolved) fluorimetry, the temperature stability of protein samples at different concentrations of salt and glycerol was compared, and then the selected conditions were used to prepare the sample for microscopy. As a result, the structure of bovine TRiC in an open conformation was obtained at 4.42 Å resolution.</description><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Biology</subject><subject>Electron microscopy</subject><subject>Life Sciences</subject><subject>Plant Sciences</subject><subject>Short Communication</subject><subject>Zoology</subject><issn>0096-3925</issn><issn>1934-791X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNp1kF9LwzAUxYMoOKcfwLeAz3X507TNo8ZNhcnATfCtJGmiHS6pSSvs25tRwQfx6V7u-Z1z4QBwidE1xYjO1gjxgnLCCC0RIpgfgQnmNM9Kjl-PweQgZwf9FJzFuEWIMU75BNyJsPfZ_Amu-zDofggGegtv_VfrDBTvsjPBu9bBzXMrZkJsYNpXnXFQeGd92Mm-9e4cnFj5Ec3Fz5yCl8V8Ix6y5er-UdwsM40ryjOiFJOksRLzwkqtLeMkN41uqlI3rFCKK1vghFZVI7FMB1IpbQplDa8KqegUXI25XfCfg4l9vfVDcOllTThjNM8xwonCI6WDjzEYW3eh3cmwrzGqD2XVf8pKHjJ6YmLdmwm_yf-bvgFEPGr9</recordid><startdate>20231201</startdate><enddate>20231201</enddate><creator>Stanishneva-Konovalova, T. B.</creator><creator>Pichkur, E. B.</creator><creator>Kudryavtseva, S. S.</creator><creator>Yaroshevich, I. A.</creator><creator>Semenov, A. N.</creator><creator>Maksimov, E. G.</creator><creator>Moiseenko, A. V.</creator><creator>Volokh, O. I.</creator><creator>Muronets, V. I.</creator><general>Pleiades Publishing</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><orcidid>https://orcid.org/0000-0003-1112-2356</orcidid><orcidid>https://orcid.org/0000-0002-8427-8178</orcidid></search><sort><creationdate>20231201</creationdate><title>Cryo-EM Structure of Bovine Chaperonin TRiC/CCT in Open Conformation</title><author>Stanishneva-Konovalova, T. B. ; Pichkur, E. B. ; Kudryavtseva, S. S. ; Yaroshevich, I. A. ; Semenov, A. N. ; Maksimov, E. G. ; Moiseenko, A. V. ; Volokh, O. I. ; Muronets, V. I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1839-2bb5a2dfa196faccf5924edcd87cd56bb9bf6118388da1a6bb28bce6bfe986ab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cell Biology</topic><topic>Electron microscopy</topic><topic>Life Sciences</topic><topic>Plant Sciences</topic><topic>Short Communication</topic><topic>Zoology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stanishneva-Konovalova, T. B.</creatorcontrib><creatorcontrib>Pichkur, E. B.</creatorcontrib><creatorcontrib>Kudryavtseva, S. S.</creatorcontrib><creatorcontrib>Yaroshevich, I. A.</creatorcontrib><creatorcontrib>Semenov, A. N.</creatorcontrib><creatorcontrib>Maksimov, E. G.</creatorcontrib><creatorcontrib>Moiseenko, A. V.</creatorcontrib><creatorcontrib>Volokh, O. I.</creatorcontrib><creatorcontrib>Muronets, V. I.</creatorcontrib><collection>CrossRef</collection><jtitle>Moscow University biological sciences bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stanishneva-Konovalova, T. B.</au><au>Pichkur, E. B.</au><au>Kudryavtseva, S. S.</au><au>Yaroshevich, I. A.</au><au>Semenov, A. N.</au><au>Maksimov, E. G.</au><au>Moiseenko, A. V.</au><au>Volokh, O. I.</au><au>Muronets, V. I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cryo-EM Structure of Bovine Chaperonin TRiC/CCT in Open Conformation</atitle><jtitle>Moscow University biological sciences bulletin</jtitle><stitle>Moscow Univ. Biol.Sci. Bull</stitle><date>2023-12-01</date><risdate>2023</risdate><volume>78</volume><issue>Suppl 1</issue><spage>S50</spage><epage>S55</epage><pages>S50-S55</pages><issn>0096-3925</issn><eissn>1934-791X</eissn><abstract>In this work, conditions were selected for obtaining a sample of eukaryotic chaperonin TRiC suitable for studying by cryo-electron microscopy. Using the method of differential scanning (time-resolved) fluorimetry, the temperature stability of protein samples at different concentrations of salt and glycerol was compared, and then the selected conditions were used to prepare the sample for microscopy. As a result, the structure of bovine TRiC in an open conformation was obtained at 4.42 Å resolution.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><doi>10.3103/S0096392523700219</doi><orcidid>https://orcid.org/0000-0003-1112-2356</orcidid><orcidid>https://orcid.org/0000-0002-8427-8178</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0096-3925 |
| ispartof | Moscow University biological sciences bulletin, 2023-12, Vol.78 (Suppl 1), p.S50-S55 |
| issn | 0096-3925 1934-791X |
| language | eng |
| recordid | cdi_proquest_journals_2955344101 |
| source | SpringerLink Journals - AutoHoldings |
| subjects | Biochemistry Biomedical and Life Sciences Cell Biology Electron microscopy Life Sciences Plant Sciences Short Communication Zoology |
| title | Cryo-EM Structure of Bovine Chaperonin TRiC/CCT in Open Conformation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T00%3A31%3A11IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cryo-EM%20Structure%20of%20Bovine%20Chaperonin%20TRiC/CCT%20in%20Open%20Conformation&rft.jtitle=Moscow%20University%20biological%20sciences%20bulletin&rft.au=Stanishneva-Konovalova,%20T.%20B.&rft.date=2023-12-01&rft.volume=78&rft.issue=Suppl%201&rft.spage=S50&rft.epage=S55&rft.pages=S50-S55&rft.issn=0096-3925&rft.eissn=1934-791X&rft_id=info:doi/10.3103/S0096392523700219&rft_dat=%3Cproquest_cross%3E2955344101%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2955344101&rft_id=info:pmid/&rfr_iscdi=true |