Rational design of lipid for membrane protein crystallization

The lipidic cubic phase has been used to grow crystals of membrane proteins for high-resolution structure determination. However, the original, so-called, in meso method does not work reliably at low temperatures, where proteins are generally more stable, because the hosting lipid turns solid. The n...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of structural biology 2004-11, Vol.148 (2), p.169-175
Hauptverfasser: Misquitta, Yohann, Cherezov, Vadim, Havas, Fabien, Patterson, Suzanne, Mohan, Jakkam M., Wells, Angela J., Hart, David J., Caffrey, Martin
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 175
container_issue 2
container_start_page 169
container_title Journal of structural biology
container_volume 148
creator Misquitta, Yohann
Cherezov, Vadim
Havas, Fabien
Patterson, Suzanne
Mohan, Jakkam M.
Wells, Angela J.
Hart, David J.
Caffrey, Martin
description The lipidic cubic phase has been used to grow crystals of membrane proteins for high-resolution structure determination. However, the original, so-called, in meso method does not work reliably at low temperatures, where proteins are generally more stable, because the hosting lipid turns solid. The need existed therefore for a lipid that forms the cubic phase and that supports crystal growth at low temperatures. We created a database of phase diagrams and used it to design such a lipid. X-ray diffraction showed that the new lipid exhibits designed phase behavior. Further, it produces diffraction quality membrane protein crystals by the in meso method at 6 °C. This demonstrates that lipidic materials, like their protein counterparts are amenable to rational design. The same approach as used in this study should find application in extending the range of membrane proteins crystallizable by the in meso method and in tailoring transport of cubic phases for controlled delivery and uptake.
doi_str_mv 10.1016/j.jsb.2004.06.008
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66965975</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1047847704001273</els_id><sourcerecordid>66965975</sourcerecordid><originalsourceid>FETCH-LOGICAL-c415t-da813b11bf4377d62e02271eaecf18287da38f3a56d8fac4145b065c1f1bc5703</originalsourceid><addsrcrecordid>eNp9kE1LxDAQhoMorq7-AC_Sk7fWTNskLeJBFr9gQRA9hzSZSEo_1qQrrL_erLvgzdOE4XlfJg8hF0AzoMCv26wNTZZTWmaUZ5RWB-QEaM3SijNxuH2XIq1KIWbkNISWRhByOCYzYHFJa3FCbl_V5MZBdYnB4D6GZLRJ51bOJHb0SY9949WAycqPE7oh0X4TJtV17vs3dkaOrOoCnu_nnLw_3L8tntLly-Pz4m6Z6hLYlBpVQdEANLYshDA8R5rnAlChtlDllTCqqGyhGDeVVTFTsoZypsFCo5mgxZxc7XrjHZ9rDJPsXdDYdfG2cR0k5zVntWARhB2o_RiCRytX3vXKbyRQuXUmWxmdya0zSbmMzmLmcl--bno0f4m9pAjc7ACMX_xy6GXQDgeNxnnUkzSj-6f-B22wfKY</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>66965975</pqid></control><display><type>article</type><title>Rational design of lipid for membrane protein crystallization</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Misquitta, Yohann ; Cherezov, Vadim ; Havas, Fabien ; Patterson, Suzanne ; Mohan, Jakkam M. ; Wells, Angela J. ; Hart, David J. ; Caffrey, Martin</creator><creatorcontrib>Misquitta, Yohann ; Cherezov, Vadim ; Havas, Fabien ; Patterson, Suzanne ; Mohan, Jakkam M. ; Wells, Angela J. ; Hart, David J. ; Caffrey, Martin</creatorcontrib><description>The lipidic cubic phase has been used to grow crystals of membrane proteins for high-resolution structure determination. However, the original, so-called, in meso method does not work reliably at low temperatures, where proteins are generally more stable, because the hosting lipid turns solid. The need existed therefore for a lipid that forms the cubic phase and that supports crystal growth at low temperatures. We created a database of phase diagrams and used it to design such a lipid. X-ray diffraction showed that the new lipid exhibits designed phase behavior. Further, it produces diffraction quality membrane protein crystals by the in meso method at 6 °C. This demonstrates that lipidic materials, like their protein counterparts are amenable to rational design. The same approach as used in this study should find application in extending the range of membrane proteins crystallizable by the in meso method and in tailoring transport of cubic phases for controlled delivery and uptake.</description><identifier>ISSN: 1047-8477</identifier><identifier>EISSN: 1095-8657</identifier><identifier>DOI: 10.1016/j.jsb.2004.06.008</identifier><identifier>PMID: 15477097</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Carbon - chemistry ; Crystallization - methods ; Crystallography, X-Ray - methods ; Cubic phase ; Glycerol - chemistry ; Halobacterium salinarum - metabolism ; Lipids - chemistry ; Membrane Proteins - chemistry ; Monoacylglycerol ; Phase diagram ; Protein Conformation ; Structure ; Temperature ; Water - chemistry ; X-Ray Diffraction</subject><ispartof>Journal of structural biology, 2004-11, Vol.148 (2), p.169-175</ispartof><rights>2004 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-da813b11bf4377d62e02271eaecf18287da38f3a56d8fac4145b065c1f1bc5703</citedby><cites>FETCH-LOGICAL-c415t-da813b11bf4377d62e02271eaecf18287da38f3a56d8fac4145b065c1f1bc5703</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1047847704001273$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15477097$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Misquitta, Yohann</creatorcontrib><creatorcontrib>Cherezov, Vadim</creatorcontrib><creatorcontrib>Havas, Fabien</creatorcontrib><creatorcontrib>Patterson, Suzanne</creatorcontrib><creatorcontrib>Mohan, Jakkam M.</creatorcontrib><creatorcontrib>Wells, Angela J.</creatorcontrib><creatorcontrib>Hart, David J.</creatorcontrib><creatorcontrib>Caffrey, Martin</creatorcontrib><title>Rational design of lipid for membrane protein crystallization</title><title>Journal of structural biology</title><addtitle>J Struct Biol</addtitle><description>The lipidic cubic phase has been used to grow crystals of membrane proteins for high-resolution structure determination. However, the original, so-called, in meso method does not work reliably at low temperatures, where proteins are generally more stable, because the hosting lipid turns solid. The need existed therefore for a lipid that forms the cubic phase and that supports crystal growth at low temperatures. We created a database of phase diagrams and used it to design such a lipid. X-ray diffraction showed that the new lipid exhibits designed phase behavior. Further, it produces diffraction quality membrane protein crystals by the in meso method at 6 °C. This demonstrates that lipidic materials, like their protein counterparts are amenable to rational design. The same approach as used in this study should find application in extending the range of membrane proteins crystallizable by the in meso method and in tailoring transport of cubic phases for controlled delivery and uptake.</description><subject>Carbon - chemistry</subject><subject>Crystallization - methods</subject><subject>Crystallography, X-Ray - methods</subject><subject>Cubic phase</subject><subject>Glycerol - chemistry</subject><subject>Halobacterium salinarum - metabolism</subject><subject>Lipids - chemistry</subject><subject>Membrane Proteins - chemistry</subject><subject>Monoacylglycerol</subject><subject>Phase diagram</subject><subject>Protein Conformation</subject><subject>Structure</subject><subject>Temperature</subject><subject>Water - chemistry</subject><subject>X-Ray Diffraction</subject><issn>1047-8477</issn><issn>1095-8657</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LxDAQhoMorq7-AC_Sk7fWTNskLeJBFr9gQRA9hzSZSEo_1qQrrL_erLvgzdOE4XlfJg8hF0AzoMCv26wNTZZTWmaUZ5RWB-QEaM3SijNxuH2XIq1KIWbkNISWRhByOCYzYHFJa3FCbl_V5MZBdYnB4D6GZLRJ51bOJHb0SY9949WAycqPE7oh0X4TJtV17vs3dkaOrOoCnu_nnLw_3L8tntLly-Pz4m6Z6hLYlBpVQdEANLYshDA8R5rnAlChtlDllTCqqGyhGDeVVTFTsoZypsFCo5mgxZxc7XrjHZ9rDJPsXdDYdfG2cR0k5zVntWARhB2o_RiCRytX3vXKbyRQuXUmWxmdya0zSbmMzmLmcl--bno0f4m9pAjc7ACMX_xy6GXQDgeNxnnUkzSj-6f-B22wfKY</recordid><startdate>20041101</startdate><enddate>20041101</enddate><creator>Misquitta, Yohann</creator><creator>Cherezov, Vadim</creator><creator>Havas, Fabien</creator><creator>Patterson, Suzanne</creator><creator>Mohan, Jakkam M.</creator><creator>Wells, Angela J.</creator><creator>Hart, David J.</creator><creator>Caffrey, Martin</creator><general>Elsevier Inc</general><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></search><sort><creationdate>20041101</creationdate><title>Rational design of lipid for membrane protein crystallization</title><author>Misquitta, Yohann ; Cherezov, Vadim ; Havas, Fabien ; Patterson, Suzanne ; Mohan, Jakkam M. ; Wells, Angela J. ; Hart, David J. ; Caffrey, Martin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-da813b11bf4377d62e02271eaecf18287da38f3a56d8fac4145b065c1f1bc5703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Carbon - chemistry</topic><topic>Crystallization - methods</topic><topic>Crystallography, X-Ray - methods</topic><topic>Cubic phase</topic><topic>Glycerol - chemistry</topic><topic>Halobacterium salinarum - metabolism</topic><topic>Lipids - chemistry</topic><topic>Membrane Proteins - chemistry</topic><topic>Monoacylglycerol</topic><topic>Phase diagram</topic><topic>Protein Conformation</topic><topic>Structure</topic><topic>Temperature</topic><topic>Water - chemistry</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Misquitta, Yohann</creatorcontrib><creatorcontrib>Cherezov, Vadim</creatorcontrib><creatorcontrib>Havas, Fabien</creatorcontrib><creatorcontrib>Patterson, Suzanne</creatorcontrib><creatorcontrib>Mohan, Jakkam M.</creatorcontrib><creatorcontrib>Wells, Angela J.</creatorcontrib><creatorcontrib>Hart, David J.</creatorcontrib><creatorcontrib>Caffrey, Martin</creatorcontrib><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><jtitle>Journal of structural biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Misquitta, Yohann</au><au>Cherezov, Vadim</au><au>Havas, Fabien</au><au>Patterson, Suzanne</au><au>Mohan, Jakkam M.</au><au>Wells, Angela J.</au><au>Hart, David J.</au><au>Caffrey, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rational design of lipid for membrane protein crystallization</atitle><jtitle>Journal of structural biology</jtitle><addtitle>J Struct Biol</addtitle><date>2004-11-01</date><risdate>2004</risdate><volume>148</volume><issue>2</issue><spage>169</spage><epage>175</epage><pages>169-175</pages><issn>1047-8477</issn><eissn>1095-8657</eissn><abstract>The lipidic cubic phase has been used to grow crystals of membrane proteins for high-resolution structure determination. However, the original, so-called, in meso method does not work reliably at low temperatures, where proteins are generally more stable, because the hosting lipid turns solid. The need existed therefore for a lipid that forms the cubic phase and that supports crystal growth at low temperatures. We created a database of phase diagrams and used it to design such a lipid. X-ray diffraction showed that the new lipid exhibits designed phase behavior. Further, it produces diffraction quality membrane protein crystals by the in meso method at 6 °C. This demonstrates that lipidic materials, like their protein counterparts are amenable to rational design. The same approach as used in this study should find application in extending the range of membrane proteins crystallizable by the in meso method and in tailoring transport of cubic phases for controlled delivery and uptake.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15477097</pmid><doi>10.1016/j.jsb.2004.06.008</doi><tpages>7</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1047-8477
ispartof Journal of structural biology, 2004-11, Vol.148 (2), p.169-175
issn 1047-8477
1095-8657
language eng
recordid cdi_proquest_miscellaneous_66965975
source MEDLINE; Elsevier ScienceDirect Journals
subjects Carbon - chemistry
Crystallization - methods
Crystallography, X-Ray - methods
Cubic phase
Glycerol - chemistry
Halobacterium salinarum - metabolism
Lipids - chemistry
Membrane Proteins - chemistry
Monoacylglycerol
Phase diagram
Protein Conformation
Structure
Temperature
Water - chemistry
X-Ray Diffraction
title Rational design of lipid for membrane protein crystallization
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-04T21%3A19%3A07IST&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=Rational%20design%20of%20lipid%20for%20membrane%20protein%20crystallization&rft.jtitle=Journal%20of%20structural%20biology&rft.au=Misquitta,%20Yohann&rft.date=2004-11-01&rft.volume=148&rft.issue=2&rft.spage=169&rft.epage=175&rft.pages=169-175&rft.issn=1047-8477&rft.eissn=1095-8657&rft_id=info:doi/10.1016/j.jsb.2004.06.008&rft_dat=%3Cproquest_cross%3E66965975%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=66965975&rft_id=info:pmid/15477097&rft_els_id=S1047847704001273&rfr_iscdi=true