Porous nucleating agents for protein crystallization
A Protocol for obtaining high-quality protein crystals that involves addition to the protein solution of solid or semi-liquid nucleants that provide the experimenter the means to control crystal growth. Solving the structure of proteins is pivotal to achieving success in rational drug design and in...
Gespeichert in:
| Veröffentlicht in: | Nature protocols 2014-07, Vol.9 (7), p.1621-1633 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1633 |
|---|---|
| container_issue | 7 |
| container_start_page | 1621 |
| container_title | Nature protocols |
| container_volume | 9 |
| creator | Khurshid, Sahir Saridakis, Emmanuel Govada, Lata Chayen, Naomi E |
| description | A Protocol for obtaining high-quality protein crystals that involves addition to the protein solution of solid or semi-liquid nucleants that provide the experimenter the means to control crystal growth.
Solving the structure of proteins is pivotal to achieving success in rational drug design and in other biotechnological endeavors. The most powerful method for determining the structure of proteins is X-ray crystallography, which relies on the availability of high-quality crystals. However, obtaining such crystals is a major hurdle. Nucleation is the crucial prerequisite step, which requires overcoming an energy barrier. The presence in a protein solution of a nucleant, a solid or a semiliquid substance that facilitates overcoming that barrier allows crystals to grow under ideal conditions, paving the way for the formation of high-quality crystals. The use of nucleants provides a unique means for optimizing the diffraction quality of crystals, as well as for discovering new crystallization conditions. We present a protocol for controlling the nucleation of protein crystals that is applicable to a wide variety of nucleation-inducing substances. Setting up crystallization trials using these nucleating agents takes an additional few seconds compared with conventional setup, and it can accelerate crystallization, which typically takes several days to months. |
| doi_str_mv | 10.1038/nprot.2014.109 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_1535622898</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A374101196</galeid><sourcerecordid>A374101196</sourcerecordid><originalsourceid>FETCH-LOGICAL-c530t-53a9bf7314d40c07a7a5e0500fa2742411860b916e10fe17f0fa89c921f0fb923</originalsourceid><addsrcrecordid>eNptkU1P3DAQhi1EVSj0yrGKxKU9ZJlxnHV8RKhQJKRWLT1bXu84Csra1HYk6K-vs9APqpUPnvE883pGL2MnCAuEpjvz9zHkBQcUJVd77BBlCzWXSu1vY1Fz7NQBe5PSHYCQzVK-ZgdcKM65xEMmvoQYplT5yY5k8uD7yvTkc6pciNUsToOvbHxM2Yzj8LMgwR-zV86Mid4-30fs--XH24tP9c3nq-uL85vatg3kum2MWjnZoFgLsCCNNC1BC-AMl4ILxG4JK4VLQnCE0pVCp6ziWKKV4s0Re_-kW-b4MVHKejMkS-NoPJWhNbZNu-S8U11BT_9D78IUfZluS4HE8s9fqjcj6cG7kKOxs6g-b6RAQFQztdhBlbOmzWCDJzeU9xcNH140FCbTQ-7NlJK-_vZ1p7iNIaVITt_HYWPio0bQs6V6a6meLS25Kg3vnjebVhta_8F_e1iAsycglZLvKf6z-m7JX-yCqPA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1535071916</pqid></control><display><type>article</type><title>Porous nucleating agents for protein crystallization</title><source>MEDLINE</source><source>Nature Journals Online</source><source>SpringerLink Journals - AutoHoldings</source><creator>Khurshid, Sahir ; Saridakis, Emmanuel ; Govada, Lata ; Chayen, Naomi E</creator><creatorcontrib>Khurshid, Sahir ; Saridakis, Emmanuel ; Govada, Lata ; Chayen, Naomi E</creatorcontrib><description>A Protocol for obtaining high-quality protein crystals that involves addition to the protein solution of solid or semi-liquid nucleants that provide the experimenter the means to control crystal growth.
Solving the structure of proteins is pivotal to achieving success in rational drug design and in other biotechnological endeavors. The most powerful method for determining the structure of proteins is X-ray crystallography, which relies on the availability of high-quality crystals. However, obtaining such crystals is a major hurdle. Nucleation is the crucial prerequisite step, which requires overcoming an energy barrier. The presence in a protein solution of a nucleant, a solid or a semiliquid substance that facilitates overcoming that barrier allows crystals to grow under ideal conditions, paving the way for the formation of high-quality crystals. The use of nucleants provides a unique means for optimizing the diffraction quality of crystals, as well as for discovering new crystallization conditions. We present a protocol for controlling the nucleation of protein crystals that is applicable to a wide variety of nucleation-inducing substances. Setting up crystallization trials using these nucleating agents takes an additional few seconds compared with conventional setup, and it can accelerate crystallization, which typically takes several days to months.</description><identifier>ISSN: 1754-2189</identifier><identifier>EISSN: 1750-2799</identifier><identifier>DOI: 10.1038/nprot.2014.109</identifier><identifier>PMID: 24922271</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/535/1266 ; Analysis ; Analytical Chemistry ; Biological Techniques ; Biotechnology ; Ceramics - chemistry ; Computational Biology/Bioinformatics ; Crystallization ; Crystallization - methods ; Crystallography ; Crystals ; Filtration ; Life Sciences ; Microarrays ; Nucleation ; Organic Chemistry ; Paving ; Phase Transition ; Porosity ; Porous materials ; Protein Stability ; Proteins ; Proteins - chemistry ; Protocol ; Structure ; Success ; Surface chemistry ; Thin films ; X-ray crystallography ; X-Ray Diffraction</subject><ispartof>Nature protocols, 2014-07, Vol.9 (7), p.1621-1633</ispartof><rights>Springer Nature Limited 2014</rights><rights>COPYRIGHT 2014 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jul 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c530t-53a9bf7314d40c07a7a5e0500fa2742411860b916e10fe17f0fa89c921f0fb923</citedby><cites>FETCH-LOGICAL-c530t-53a9bf7314d40c07a7a5e0500fa2742411860b916e10fe17f0fa89c921f0fb923</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nprot.2014.109$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nprot.2014.109$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24922271$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Khurshid, Sahir</creatorcontrib><creatorcontrib>Saridakis, Emmanuel</creatorcontrib><creatorcontrib>Govada, Lata</creatorcontrib><creatorcontrib>Chayen, Naomi E</creatorcontrib><title>Porous nucleating agents for protein crystallization</title><title>Nature protocols</title><addtitle>Nat Protoc</addtitle><addtitle>Nat Protoc</addtitle><description>A Protocol for obtaining high-quality protein crystals that involves addition to the protein solution of solid or semi-liquid nucleants that provide the experimenter the means to control crystal growth.
Solving the structure of proteins is pivotal to achieving success in rational drug design and in other biotechnological endeavors. The most powerful method for determining the structure of proteins is X-ray crystallography, which relies on the availability of high-quality crystals. However, obtaining such crystals is a major hurdle. Nucleation is the crucial prerequisite step, which requires overcoming an energy barrier. The presence in a protein solution of a nucleant, a solid or a semiliquid substance that facilitates overcoming that barrier allows crystals to grow under ideal conditions, paving the way for the formation of high-quality crystals. The use of nucleants provides a unique means for optimizing the diffraction quality of crystals, as well as for discovering new crystallization conditions. We present a protocol for controlling the nucleation of protein crystals that is applicable to a wide variety of nucleation-inducing substances. Setting up crystallization trials using these nucleating agents takes an additional few seconds compared with conventional setup, and it can accelerate crystallization, which typically takes several days to months.</description><subject>631/535/1266</subject><subject>Analysis</subject><subject>Analytical Chemistry</subject><subject>Biological Techniques</subject><subject>Biotechnology</subject><subject>Ceramics - chemistry</subject><subject>Computational Biology/Bioinformatics</subject><subject>Crystallization</subject><subject>Crystallization - methods</subject><subject>Crystallography</subject><subject>Crystals</subject><subject>Filtration</subject><subject>Life Sciences</subject><subject>Microarrays</subject><subject>Nucleation</subject><subject>Organic Chemistry</subject><subject>Paving</subject><subject>Phase Transition</subject><subject>Porosity</subject><subject>Porous materials</subject><subject>Protein Stability</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Protocol</subject><subject>Structure</subject><subject>Success</subject><subject>Surface chemistry</subject><subject>Thin films</subject><subject>X-ray crystallography</subject><subject>X-Ray Diffraction</subject><issn>1754-2189</issn><issn>1750-2799</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><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>eNptkU1P3DAQhi1EVSj0yrGKxKU9ZJlxnHV8RKhQJKRWLT1bXu84Csra1HYk6K-vs9APqpUPnvE883pGL2MnCAuEpjvz9zHkBQcUJVd77BBlCzWXSu1vY1Fz7NQBe5PSHYCQzVK-ZgdcKM65xEMmvoQYplT5yY5k8uD7yvTkc6pciNUsToOvbHxM2Yzj8LMgwR-zV86Mid4-30fs--XH24tP9c3nq-uL85vatg3kum2MWjnZoFgLsCCNNC1BC-AMl4ILxG4JK4VLQnCE0pVCp6ziWKKV4s0Re_-kW-b4MVHKejMkS-NoPJWhNbZNu-S8U11BT_9D78IUfZluS4HE8s9fqjcj6cG7kKOxs6g-b6RAQFQztdhBlbOmzWCDJzeU9xcNH140FCbTQ-7NlJK-_vZ1p7iNIaVITt_HYWPio0bQs6V6a6meLS25Kg3vnjebVhta_8F_e1iAsycglZLvKf6z-m7JX-yCqPA</recordid><startdate>20140701</startdate><enddate>20140701</enddate><creator>Khurshid, Sahir</creator><creator>Saridakis, Emmanuel</creator><creator>Govada, Lata</creator><creator>Chayen, Naomi E</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</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>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7T5</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20140701</creationdate><title>Porous nucleating agents for protein crystallization</title><author>Khurshid, Sahir ; Saridakis, Emmanuel ; Govada, Lata ; Chayen, Naomi E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c530t-53a9bf7314d40c07a7a5e0500fa2742411860b916e10fe17f0fa89c921f0fb923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>631/535/1266</topic><topic>Analysis</topic><topic>Analytical Chemistry</topic><topic>Biological Techniques</topic><topic>Biotechnology</topic><topic>Ceramics - chemistry</topic><topic>Computational Biology/Bioinformatics</topic><topic>Crystallization</topic><topic>Crystallization - methods</topic><topic>Crystallography</topic><topic>Crystals</topic><topic>Filtration</topic><topic>Life Sciences</topic><topic>Microarrays</topic><topic>Nucleation</topic><topic>Organic Chemistry</topic><topic>Paving</topic><topic>Phase Transition</topic><topic>Porosity</topic><topic>Porous materials</topic><topic>Protein Stability</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Protocol</topic><topic>Structure</topic><topic>Success</topic><topic>Surface chemistry</topic><topic>Thin films</topic><topic>X-ray crystallography</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Khurshid, Sahir</creatorcontrib><creatorcontrib>Saridakis, Emmanuel</creatorcontrib><creatorcontrib>Govada, Lata</creatorcontrib><creatorcontrib>Chayen, Naomi E</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</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 One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature protocols</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Khurshid, Sahir</au><au>Saridakis, Emmanuel</au><au>Govada, Lata</au><au>Chayen, Naomi E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Porous nucleating agents for protein crystallization</atitle><jtitle>Nature protocols</jtitle><stitle>Nat Protoc</stitle><addtitle>Nat Protoc</addtitle><date>2014-07-01</date><risdate>2014</risdate><volume>9</volume><issue>7</issue><spage>1621</spage><epage>1633</epage><pages>1621-1633</pages><issn>1754-2189</issn><eissn>1750-2799</eissn><abstract>A Protocol for obtaining high-quality protein crystals that involves addition to the protein solution of solid or semi-liquid nucleants that provide the experimenter the means to control crystal growth.
Solving the structure of proteins is pivotal to achieving success in rational drug design and in other biotechnological endeavors. The most powerful method for determining the structure of proteins is X-ray crystallography, which relies on the availability of high-quality crystals. However, obtaining such crystals is a major hurdle. Nucleation is the crucial prerequisite step, which requires overcoming an energy barrier. The presence in a protein solution of a nucleant, a solid or a semiliquid substance that facilitates overcoming that barrier allows crystals to grow under ideal conditions, paving the way for the formation of high-quality crystals. The use of nucleants provides a unique means for optimizing the diffraction quality of crystals, as well as for discovering new crystallization conditions. We present a protocol for controlling the nucleation of protein crystals that is applicable to a wide variety of nucleation-inducing substances. Setting up crystallization trials using these nucleating agents takes an additional few seconds compared with conventional setup, and it can accelerate crystallization, which typically takes several days to months.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>24922271</pmid><doi>10.1038/nprot.2014.109</doi><tpages>13</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1754-2189 |
| ispartof | Nature protocols, 2014-07, Vol.9 (7), p.1621-1633 |
| issn | 1754-2189 1750-2799 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1535622898 |
| source | MEDLINE; Nature Journals Online; SpringerLink Journals - AutoHoldings |
| subjects | 631/535/1266 Analysis Analytical Chemistry Biological Techniques Biotechnology Ceramics - chemistry Computational Biology/Bioinformatics Crystallization Crystallization - methods Crystallography Crystals Filtration Life Sciences Microarrays Nucleation Organic Chemistry Paving Phase Transition Porosity Porous materials Protein Stability Proteins Proteins - chemistry Protocol Structure Success Surface chemistry Thin films X-ray crystallography X-Ray Diffraction |
| title | Porous nucleating agents for protein crystallization |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T03%3A03%3A11IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Porous%20nucleating%20agents%20for%20protein%20crystallization&rft.jtitle=Nature%20protocols&rft.au=Khurshid,%20Sahir&rft.date=2014-07-01&rft.volume=9&rft.issue=7&rft.spage=1621&rft.epage=1633&rft.pages=1621-1633&rft.issn=1754-2189&rft.eissn=1750-2799&rft_id=info:doi/10.1038/nprot.2014.109&rft_dat=%3Cgale_proqu%3EA374101196%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1535071916&rft_id=info:pmid/24922271&rft_galeid=A374101196&rfr_iscdi=true |