Three-dimensional super-resolution protein localization correlated with vitrified cellular context
We demonstrate the use of cryogenic super-resolution correlative light and electron microscopy (csCLEM) to precisely determine the spatial relationship between proteins and their native cellular structures. Several fluorescent proteins (FPs) were found to be photoswitchable and emitted far more phot...
Gespeichert in:
| Veröffentlicht in: | Scientific reports 2015-10, Vol.5 (1), p.13017-13017, Article 13017 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 13017 |
|---|---|
| container_issue | 1 |
| container_start_page | 13017 |
| container_title | Scientific reports |
| container_volume | 5 |
| creator | Liu, Bei Xue, Yanhong Zhao, Wei Chen, Yan Fan, Chunyan Gu, Lusheng Zhang, Yongdeng Zhang, Xiang Sun, Lei Huang, Xiaojun Ding, Wei Sun, Fei Ji, Wei Xu, Tao |
| description | We demonstrate the use of cryogenic super-resolution correlative light and electron microscopy (csCLEM) to precisely determine the spatial relationship between proteins and their native cellular structures. Several fluorescent proteins (FPs) were found to be photoswitchable and emitted far more photons under our cryogenic imaging condition, resulting in higher localization precision which is comparable to ambient super-resolution imaging. Vitrified specimens were prepared by high pressure freezing and cryo-sectioning to maintain a near-native state with better fluorescence preservation. A 2-3-fold improvement of resolution over the recent reports was achieved due to the photon budget performance of screening out Dronpa and optimized imaging conditions, even with thin sections which is at a disadvantage when calculate the structure resolution from label density. We extended csCLEM to mammalian cells by introducing cryo-sectioning and observed good correlation of a mitochondrial protein with the mitochondrial outer membrane at nanometer resolution in three dimensions. |
| doi_str_mv | 10.1038/srep13017 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4604464</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1722420747</sourcerecordid><originalsourceid>FETCH-LOGICAL-c438t-29a6e93cf649c4f58610c4e422a72445d2bc83625e55bf581756d3896d34266f3</originalsourceid><addsrcrecordid>eNplkU1rFTEUhoMottQu_AMy4EaFsfk4SWY2gpTWCoVu6jrkZs70puROxiTTqr_e1NterppFPs778OYkLyGvGf3IqOhOcsKZCcr0M3LIKciWC86f7-0PyHHOt7QOyXtg_UtywBUo3unukKyu1wmxHfwGp-zjZEOTlxlTmzDHsJRaauYUC_qpCdHZ4H_ZP0UXU8JgCw7NvS_r5s6X5Edfjw5DWIJNFZkK_iivyIvRhozHj-sR-XZ-dn160V5effl6-vmydSC60vLeKuyFGxX0DkbZKUYdIHBuNQeQA1-5TiguUcpVlZmWahBdXyfgSo3iiHza-s7LaoODw6kkG8yc_MamnyZab_5WJr82N_HOgKIACqrBu0eDFL8vmIvZ-PzwGjthXLJhmnPgVIOu6Nt_0Nu4pPp7ler6XmshBa3U-y3lUsw1p3HXDKPmITyzC6-yb_a735FPUVXgwxbIVZpuMO1d-Z_bbziapS8</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1899773530</pqid></control><display><type>article</type><title>Three-dimensional super-resolution protein localization correlated with vitrified cellular context</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Springer Nature OA Free Journals</source><source>Nature Free</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Liu, Bei ; Xue, Yanhong ; Zhao, Wei ; Chen, Yan ; Fan, Chunyan ; Gu, Lusheng ; Zhang, Yongdeng ; Zhang, Xiang ; Sun, Lei ; Huang, Xiaojun ; Ding, Wei ; Sun, Fei ; Ji, Wei ; Xu, Tao</creator><creatorcontrib>Liu, Bei ; Xue, Yanhong ; Zhao, Wei ; Chen, Yan ; Fan, Chunyan ; Gu, Lusheng ; Zhang, Yongdeng ; Zhang, Xiang ; Sun, Lei ; Huang, Xiaojun ; Ding, Wei ; Sun, Fei ; Ji, Wei ; Xu, Tao</creatorcontrib><description>We demonstrate the use of cryogenic super-resolution correlative light and electron microscopy (csCLEM) to precisely determine the spatial relationship between proteins and their native cellular structures. Several fluorescent proteins (FPs) were found to be photoswitchable and emitted far more photons under our cryogenic imaging condition, resulting in higher localization precision which is comparable to ambient super-resolution imaging. Vitrified specimens were prepared by high pressure freezing and cryo-sectioning to maintain a near-native state with better fluorescence preservation. A 2-3-fold improvement of resolution over the recent reports was achieved due to the photon budget performance of screening out Dronpa and optimized imaging conditions, even with thin sections which is at a disadvantage when calculate the structure resolution from label density. We extended csCLEM to mammalian cells by introducing cryo-sectioning and observed good correlation of a mitochondrial protein with the mitochondrial outer membrane at nanometer resolution in three dimensions.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep13017</identifier><identifier>PMID: 26462878</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/57/2265 ; 631/57/2282 ; Cryopreservation - instrumentation ; Cryopreservation - methods ; Electron microscopy ; Equipment Design ; Equipment Failure Analysis ; Freezing ; HEK293 Cells ; High pressure ; Humanities and Social Sciences ; Humans ; Image Enhancement - instrumentation ; Image Enhancement - methods ; Imaging, Three-Dimensional - instrumentation ; Imaging, Three-Dimensional - methods ; Localization ; Mammalian cells ; Micro-Electrical-Mechanical Systems - instrumentation ; Micro-Electrical-Mechanical Systems - methods ; Microscopy, Electron - instrumentation ; Microscopy, Fluorescence - instrumentation ; Microscopy, Fluorescence - methods ; Mitochondria ; Molecular Imaging - instrumentation ; Molecular Imaging - methods ; multidisciplinary ; Multimodal Imaging - instrumentation ; Multimodal Imaging - methods ; Preservation ; Proteins - metabolism ; Reproducibility of Results ; Science ; Sectioning ; Sensitivity and Specificity ; Statistics as Topic ; Subcellular Fractions - metabolism ; Tissue Distribution ; Vitrification</subject><ispartof>Scientific reports, 2015-10, Vol.5 (1), p.13017-13017, Article 13017</ispartof><rights>The Author(s) 2015</rights><rights>Copyright Nature Publishing Group Oct 2015</rights><rights>Copyright © 2015, Macmillan Publishers Limited 2015 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-29a6e93cf649c4f58610c4e422a72445d2bc83625e55bf581756d3896d34266f3</citedby><cites>FETCH-LOGICAL-c438t-29a6e93cf649c4f58610c4e422a72445d2bc83625e55bf581756d3896d34266f3</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/PMC4604464/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4604464/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,27929,27930,41125,42194,51581,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26462878$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Bei</creatorcontrib><creatorcontrib>Xue, Yanhong</creatorcontrib><creatorcontrib>Zhao, Wei</creatorcontrib><creatorcontrib>Chen, Yan</creatorcontrib><creatorcontrib>Fan, Chunyan</creatorcontrib><creatorcontrib>Gu, Lusheng</creatorcontrib><creatorcontrib>Zhang, Yongdeng</creatorcontrib><creatorcontrib>Zhang, Xiang</creatorcontrib><creatorcontrib>Sun, Lei</creatorcontrib><creatorcontrib>Huang, Xiaojun</creatorcontrib><creatorcontrib>Ding, Wei</creatorcontrib><creatorcontrib>Sun, Fei</creatorcontrib><creatorcontrib>Ji, Wei</creatorcontrib><creatorcontrib>Xu, Tao</creatorcontrib><title>Three-dimensional super-resolution protein localization correlated with vitrified cellular context</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>We demonstrate the use of cryogenic super-resolution correlative light and electron microscopy (csCLEM) to precisely determine the spatial relationship between proteins and their native cellular structures. Several fluorescent proteins (FPs) were found to be photoswitchable and emitted far more photons under our cryogenic imaging condition, resulting in higher localization precision which is comparable to ambient super-resolution imaging. Vitrified specimens were prepared by high pressure freezing and cryo-sectioning to maintain a near-native state with better fluorescence preservation. A 2-3-fold improvement of resolution over the recent reports was achieved due to the photon budget performance of screening out Dronpa and optimized imaging conditions, even with thin sections which is at a disadvantage when calculate the structure resolution from label density. We extended csCLEM to mammalian cells by introducing cryo-sectioning and observed good correlation of a mitochondrial protein with the mitochondrial outer membrane at nanometer resolution in three dimensions.</description><subject>631/57/2265</subject><subject>631/57/2282</subject><subject>Cryopreservation - instrumentation</subject><subject>Cryopreservation - methods</subject><subject>Electron microscopy</subject><subject>Equipment Design</subject><subject>Equipment Failure Analysis</subject><subject>Freezing</subject><subject>HEK293 Cells</subject><subject>High pressure</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Image Enhancement - instrumentation</subject><subject>Image Enhancement - methods</subject><subject>Imaging, Three-Dimensional - instrumentation</subject><subject>Imaging, Three-Dimensional - methods</subject><subject>Localization</subject><subject>Mammalian cells</subject><subject>Micro-Electrical-Mechanical Systems - instrumentation</subject><subject>Micro-Electrical-Mechanical Systems - methods</subject><subject>Microscopy, Electron - instrumentation</subject><subject>Microscopy, Fluorescence - instrumentation</subject><subject>Microscopy, Fluorescence - methods</subject><subject>Mitochondria</subject><subject>Molecular Imaging - instrumentation</subject><subject>Molecular Imaging - methods</subject><subject>multidisciplinary</subject><subject>Multimodal Imaging - instrumentation</subject><subject>Multimodal Imaging - methods</subject><subject>Preservation</subject><subject>Proteins - metabolism</subject><subject>Reproducibility of Results</subject><subject>Science</subject><subject>Sectioning</subject><subject>Sensitivity and Specificity</subject><subject>Statistics as Topic</subject><subject>Subcellular Fractions - metabolism</subject><subject>Tissue Distribution</subject><subject>Vitrification</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNplkU1rFTEUhoMottQu_AMy4EaFsfk4SWY2gpTWCoVu6jrkZs70puROxiTTqr_e1NterppFPs778OYkLyGvGf3IqOhOcsKZCcr0M3LIKciWC86f7-0PyHHOt7QOyXtg_UtywBUo3unukKyu1wmxHfwGp-zjZEOTlxlTmzDHsJRaauYUC_qpCdHZ4H_ZP0UXU8JgCw7NvS_r5s6X5Edfjw5DWIJNFZkK_iivyIvRhozHj-sR-XZ-dn160V5effl6-vmydSC60vLeKuyFGxX0DkbZKUYdIHBuNQeQA1-5TiguUcpVlZmWahBdXyfgSo3iiHza-s7LaoODw6kkG8yc_MamnyZab_5WJr82N_HOgKIACqrBu0eDFL8vmIvZ-PzwGjthXLJhmnPgVIOu6Nt_0Nu4pPp7ler6XmshBa3U-y3lUsw1p3HXDKPmITyzC6-yb_a735FPUVXgwxbIVZpuMO1d-Z_bbziapS8</recordid><startdate>20151014</startdate><enddate>20151014</enddate><creator>Liu, Bei</creator><creator>Xue, Yanhong</creator><creator>Zhao, Wei</creator><creator>Chen, Yan</creator><creator>Fan, Chunyan</creator><creator>Gu, Lusheng</creator><creator>Zhang, Yongdeng</creator><creator>Zhang, Xiang</creator><creator>Sun, Lei</creator><creator>Huang, Xiaojun</creator><creator>Ding, Wei</creator><creator>Sun, Fei</creator><creator>Ji, Wei</creator><creator>Xu, Tao</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20151014</creationdate><title>Three-dimensional super-resolution protein localization correlated with vitrified cellular context</title><author>Liu, Bei ; Xue, Yanhong ; Zhao, Wei ; Chen, Yan ; Fan, Chunyan ; Gu, Lusheng ; Zhang, Yongdeng ; Zhang, Xiang ; Sun, Lei ; Huang, Xiaojun ; Ding, Wei ; Sun, Fei ; Ji, Wei ; Xu, Tao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-29a6e93cf649c4f58610c4e422a72445d2bc83625e55bf581756d3896d34266f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>631/57/2265</topic><topic>631/57/2282</topic><topic>Cryopreservation - instrumentation</topic><topic>Cryopreservation - methods</topic><topic>Electron microscopy</topic><topic>Equipment Design</topic><topic>Equipment Failure Analysis</topic><topic>Freezing</topic><topic>HEK293 Cells</topic><topic>High pressure</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Image Enhancement - instrumentation</topic><topic>Image Enhancement - methods</topic><topic>Imaging, Three-Dimensional - instrumentation</topic><topic>Imaging, Three-Dimensional - methods</topic><topic>Localization</topic><topic>Mammalian cells</topic><topic>Micro-Electrical-Mechanical Systems - instrumentation</topic><topic>Micro-Electrical-Mechanical Systems - methods</topic><topic>Microscopy, Electron - instrumentation</topic><topic>Microscopy, Fluorescence - instrumentation</topic><topic>Microscopy, Fluorescence - methods</topic><topic>Mitochondria</topic><topic>Molecular Imaging - instrumentation</topic><topic>Molecular Imaging - methods</topic><topic>multidisciplinary</topic><topic>Multimodal Imaging - instrumentation</topic><topic>Multimodal Imaging - methods</topic><topic>Preservation</topic><topic>Proteins - metabolism</topic><topic>Reproducibility of Results</topic><topic>Science</topic><topic>Sectioning</topic><topic>Sensitivity and Specificity</topic><topic>Statistics as Topic</topic><topic>Subcellular Fractions - metabolism</topic><topic>Tissue Distribution</topic><topic>Vitrification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Bei</creatorcontrib><creatorcontrib>Xue, Yanhong</creatorcontrib><creatorcontrib>Zhao, Wei</creatorcontrib><creatorcontrib>Chen, Yan</creatorcontrib><creatorcontrib>Fan, Chunyan</creatorcontrib><creatorcontrib>Gu, Lusheng</creatorcontrib><creatorcontrib>Zhang, Yongdeng</creatorcontrib><creatorcontrib>Zhang, Xiang</creatorcontrib><creatorcontrib>Sun, Lei</creatorcontrib><creatorcontrib>Huang, Xiaojun</creatorcontrib><creatorcontrib>Ding, Wei</creatorcontrib><creatorcontrib>Sun, Fei</creatorcontrib><creatorcontrib>Ji, Wei</creatorcontrib><creatorcontrib>Xu, Tao</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Access via ProQuest (Open Access)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Bei</au><au>Xue, Yanhong</au><au>Zhao, Wei</au><au>Chen, Yan</au><au>Fan, Chunyan</au><au>Gu, Lusheng</au><au>Zhang, Yongdeng</au><au>Zhang, Xiang</au><au>Sun, Lei</au><au>Huang, Xiaojun</au><au>Ding, Wei</au><au>Sun, Fei</au><au>Ji, Wei</au><au>Xu, Tao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three-dimensional super-resolution protein localization correlated with vitrified cellular context</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2015-10-14</date><risdate>2015</risdate><volume>5</volume><issue>1</issue><spage>13017</spage><epage>13017</epage><pages>13017-13017</pages><artnum>13017</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>We demonstrate the use of cryogenic super-resolution correlative light and electron microscopy (csCLEM) to precisely determine the spatial relationship between proteins and their native cellular structures. Several fluorescent proteins (FPs) were found to be photoswitchable and emitted far more photons under our cryogenic imaging condition, resulting in higher localization precision which is comparable to ambient super-resolution imaging. Vitrified specimens were prepared by high pressure freezing and cryo-sectioning to maintain a near-native state with better fluorescence preservation. A 2-3-fold improvement of resolution over the recent reports was achieved due to the photon budget performance of screening out Dronpa and optimized imaging conditions, even with thin sections which is at a disadvantage when calculate the structure resolution from label density. We extended csCLEM to mammalian cells by introducing cryo-sectioning and observed good correlation of a mitochondrial protein with the mitochondrial outer membrane at nanometer resolution in three dimensions.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>26462878</pmid><doi>10.1038/srep13017</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2045-2322 |
| ispartof | Scientific reports, 2015-10, Vol.5 (1), p.13017-13017, Article 13017 |
| issn | 2045-2322 2045-2322 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4604464 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Springer Nature OA Free Journals; Nature Free; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | 631/57/2265 631/57/2282 Cryopreservation - instrumentation Cryopreservation - methods Electron microscopy Equipment Design Equipment Failure Analysis Freezing HEK293 Cells High pressure Humanities and Social Sciences Humans Image Enhancement - instrumentation Image Enhancement - methods Imaging, Three-Dimensional - instrumentation Imaging, Three-Dimensional - methods Localization Mammalian cells Micro-Electrical-Mechanical Systems - instrumentation Micro-Electrical-Mechanical Systems - methods Microscopy, Electron - instrumentation Microscopy, Fluorescence - instrumentation Microscopy, Fluorescence - methods Mitochondria Molecular Imaging - instrumentation Molecular Imaging - methods multidisciplinary Multimodal Imaging - instrumentation Multimodal Imaging - methods Preservation Proteins - metabolism Reproducibility of Results Science Sectioning Sensitivity and Specificity Statistics as Topic Subcellular Fractions - metabolism Tissue Distribution Vitrification |
| title | Three-dimensional super-resolution protein localization correlated with vitrified cellular context |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-16T12%3A39%3A05IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Three-dimensional%20super-resolution%20protein%20localization%20correlated%20with%20vitrified%20cellular%20context&rft.jtitle=Scientific%20reports&rft.au=Liu,%20Bei&rft.date=2015-10-14&rft.volume=5&rft.issue=1&rft.spage=13017&rft.epage=13017&rft.pages=13017-13017&rft.artnum=13017&rft.issn=2045-2322&rft.eissn=2045-2322&rft_id=info:doi/10.1038/srep13017&rft_dat=%3Cproquest_pubme%3E1722420747%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1899773530&rft_id=info:pmid/26462878&rfr_iscdi=true |