Loading…
Crystals of Acetylated SecB Diffract to 2.3-Å Resolution
The molecular chaperone SecB is part of the protein translocation pathway in Escherichia coli. SecB was purified from an overproducing strain and crystallized, resulting in crystals diffracting to 2.3-Å resolution. The analysis of electrospray ionization mass spectra of dissolved crystals of SecB in...
Saved in:
| Published in: | Journal of structural biology 1999-12, Vol.128 (3), p.237-242 |
|---|---|
| Main Authors: | , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c255t-f9369d64ea97bb8da686ec493f8bf090b716473a5b86a0c48b52cbf63232c0393 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c255t-f9369d64ea97bb8da686ec493f8bf090b716473a5b86a0c48b52cbf63232c0393 |
| container_end_page | 242 |
| container_issue | 3 |
| container_start_page | 237 |
| container_title | Journal of structural biology |
| container_volume | 128 |
| creator | Dekker, Carien de Kruijff, Ben de Korte-Kool, Gerda Kroon, Jan Gros, Piet |
| description | The molecular chaperone SecB is part of the protein translocation pathway in Escherichia coli. SecB was purified from an overproducing strain and crystallized, resulting in crystals diffracting to 2.3-Å resolution. The analysis of electrospray ionization mass spectra of dissolved crystals of SecB indicated that we have crystallized an acetylated form of SecB. Sequence analysis suggests that the protein is fully acetylated at its N-terminus in vivo, indicating that potential deacetylation is artificially introduced by purification methods. The high degree of acetylation that we observed might account for the fact that the crystals obtained as described in this study diffract to higher resolution than those in previously reported trials. |
| doi_str_mv | 10.1006/jsbi.1999.4179 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69405028</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1047847799941795</els_id><sourcerecordid>69405028</sourcerecordid><originalsourceid>FETCH-LOGICAL-c255t-f9369d64ea97bb8da686ec493f8bf090b716473a5b86a0c48b52cbf63232c0393</originalsourceid><addsrcrecordid>eNp1kL1OwzAUhS0EoqWwMqJMbAl27Dj2WMqvVAmJn9mynWvJVdoU20HqA_BkvBiJ2oGF6Z7hO0e6H0KXBBcEY36zisYXREpZMFLLIzQlWFa54FV9PGZW54LV9QSdxbjCGDNSklM0IZhTink5RXIRdjHpNmady-YW0q7VCZrsDextduedC9qmLHVZWdD85zt7hdi1ffLd5hyduKEHF4c7Qx8P9--Lp3z58vi8mC9zW1ZVyp2kXDacgZa1MaLRXHCwTFInjMMSm5pwVlNdGcE1tkyYqrTGcVrS0mIq6Qxd73e3ofvsISa19tFC2-oNdH1UXDJc4VIMYLEHbehiDODUNvi1DjtFsBplqVGWGmWpUdZQuDos92YNzR98b2cAxB6A4b8vD0FF62FjofEBbFJN5__b_gWwcHdH</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69405028</pqid></control><display><type>article</type><title>Crystals of Acetylated SecB Diffract to 2.3-Å Resolution</title><source>ScienceDirect Freedom Collection 2022-2024</source><creator>Dekker, Carien ; de Kruijff, Ben ; de Korte-Kool, Gerda ; Kroon, Jan ; Gros, Piet</creator><creatorcontrib>Dekker, Carien ; de Kruijff, Ben ; de Korte-Kool, Gerda ; Kroon, Jan ; Gros, Piet</creatorcontrib><description>The molecular chaperone SecB is part of the protein translocation pathway in Escherichia coli. SecB was purified from an overproducing strain and crystallized, resulting in crystals diffracting to 2.3-Å resolution. The analysis of electrospray ionization mass spectra of dissolved crystals of SecB indicated that we have crystallized an acetylated form of SecB. Sequence analysis suggests that the protein is fully acetylated at its N-terminus in vivo, indicating that potential deacetylation is artificially introduced by purification methods. The high degree of acetylation that we observed might account for the fact that the crystals obtained as described in this study diffract to higher resolution than those in previously reported trials.</description><identifier>ISSN: 1047-8477</identifier><identifier>EISSN: 1095-8657</identifier><identifier>DOI: 10.1006/jsbi.1999.4179</identifier><identifier>PMID: 10633062</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetylation ; Bacterial Proteins - chemistry ; chaperone ; crystallization ; Crystallography ; Dithiothreitol - metabolism ; electrospray ionization mass spectrometry ; Escherichia coli - chemistry ; Mass Spectrometry ; Molecular Chaperones - chemistry ; Protein Conformation ; Protein Folding ; SecB ; X-Ray Diffraction</subject><ispartof>Journal of structural biology, 1999-12, Vol.128 (3), p.237-242</ispartof><rights>1999 Academic Press</rights><rights>Copyright 1999 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c255t-f9369d64ea97bb8da686ec493f8bf090b716473a5b86a0c48b52cbf63232c0393</citedby><cites>FETCH-LOGICAL-c255t-f9369d64ea97bb8da686ec493f8bf090b716473a5b86a0c48b52cbf63232c0393</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10633062$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dekker, Carien</creatorcontrib><creatorcontrib>de Kruijff, Ben</creatorcontrib><creatorcontrib>de Korte-Kool, Gerda</creatorcontrib><creatorcontrib>Kroon, Jan</creatorcontrib><creatorcontrib>Gros, Piet</creatorcontrib><title>Crystals of Acetylated SecB Diffract to 2.3-Å Resolution</title><title>Journal of structural biology</title><addtitle>J Struct Biol</addtitle><description>The molecular chaperone SecB is part of the protein translocation pathway in Escherichia coli. SecB was purified from an overproducing strain and crystallized, resulting in crystals diffracting to 2.3-Å resolution. The analysis of electrospray ionization mass spectra of dissolved crystals of SecB indicated that we have crystallized an acetylated form of SecB. Sequence analysis suggests that the protein is fully acetylated at its N-terminus in vivo, indicating that potential deacetylation is artificially introduced by purification methods. The high degree of acetylation that we observed might account for the fact that the crystals obtained as described in this study diffract to higher resolution than those in previously reported trials.</description><subject>Acetylation</subject><subject>Bacterial Proteins - chemistry</subject><subject>chaperone</subject><subject>crystallization</subject><subject>Crystallography</subject><subject>Dithiothreitol - metabolism</subject><subject>electrospray ionization mass spectrometry</subject><subject>Escherichia coli - chemistry</subject><subject>Mass Spectrometry</subject><subject>Molecular Chaperones - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>SecB</subject><subject>X-Ray Diffraction</subject><issn>1047-8477</issn><issn>1095-8657</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNp1kL1OwzAUhS0EoqWwMqJMbAl27Dj2WMqvVAmJn9mynWvJVdoU20HqA_BkvBiJ2oGF6Z7hO0e6H0KXBBcEY36zisYXREpZMFLLIzQlWFa54FV9PGZW54LV9QSdxbjCGDNSklM0IZhTink5RXIRdjHpNmady-YW0q7VCZrsDextduedC9qmLHVZWdD85zt7hdi1ffLd5hyduKEHF4c7Qx8P9--Lp3z58vi8mC9zW1ZVyp2kXDacgZa1MaLRXHCwTFInjMMSm5pwVlNdGcE1tkyYqrTGcVrS0mIq6Qxd73e3ofvsISa19tFC2-oNdH1UXDJc4VIMYLEHbehiDODUNvi1DjtFsBplqVGWGmWpUdZQuDos92YNzR98b2cAxB6A4b8vD0FF62FjofEBbFJN5__b_gWwcHdH</recordid><startdate>19991230</startdate><enddate>19991230</enddate><creator>Dekker, Carien</creator><creator>de Kruijff, Ben</creator><creator>de Korte-Kool, Gerda</creator><creator>Kroon, Jan</creator><creator>Gros, Piet</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>19991230</creationdate><title>Crystals of Acetylated SecB Diffract to 2.3-Å Resolution</title><author>Dekker, Carien ; de Kruijff, Ben ; de Korte-Kool, Gerda ; Kroon, Jan ; Gros, Piet</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c255t-f9369d64ea97bb8da686ec493f8bf090b716473a5b86a0c48b52cbf63232c0393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Acetylation</topic><topic>Bacterial Proteins - chemistry</topic><topic>chaperone</topic><topic>crystallization</topic><topic>Crystallography</topic><topic>Dithiothreitol - metabolism</topic><topic>electrospray ionization mass spectrometry</topic><topic>Escherichia coli - chemistry</topic><topic>Mass Spectrometry</topic><topic>Molecular Chaperones - chemistry</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>SecB</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dekker, Carien</creatorcontrib><creatorcontrib>de Kruijff, Ben</creatorcontrib><creatorcontrib>de Korte-Kool, Gerda</creatorcontrib><creatorcontrib>Kroon, Jan</creatorcontrib><creatorcontrib>Gros, Piet</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>Dekker, Carien</au><au>de Kruijff, Ben</au><au>de Korte-Kool, Gerda</au><au>Kroon, Jan</au><au>Gros, Piet</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystals of Acetylated SecB Diffract to 2.3-Å Resolution</atitle><jtitle>Journal of structural biology</jtitle><addtitle>J Struct Biol</addtitle><date>1999-12-30</date><risdate>1999</risdate><volume>128</volume><issue>3</issue><spage>237</spage><epage>242</epage><pages>237-242</pages><issn>1047-8477</issn><eissn>1095-8657</eissn><abstract>The molecular chaperone SecB is part of the protein translocation pathway in Escherichia coli. SecB was purified from an overproducing strain and crystallized, resulting in crystals diffracting to 2.3-Å resolution. The analysis of electrospray ionization mass spectra of dissolved crystals of SecB indicated that we have crystallized an acetylated form of SecB. Sequence analysis suggests that the protein is fully acetylated at its N-terminus in vivo, indicating that potential deacetylation is artificially introduced by purification methods. The high degree of acetylation that we observed might account for the fact that the crystals obtained as described in this study diffract to higher resolution than those in previously reported trials.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10633062</pmid><doi>10.1006/jsbi.1999.4179</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1047-8477 |
| ispartof | Journal of structural biology, 1999-12, Vol.128 (3), p.237-242 |
| issn | 1047-8477 1095-8657 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69405028 |
| source | ScienceDirect Freedom Collection 2022-2024 |
| subjects | Acetylation Bacterial Proteins - chemistry chaperone crystallization Crystallography Dithiothreitol - metabolism electrospray ionization mass spectrometry Escherichia coli - chemistry Mass Spectrometry Molecular Chaperones - chemistry Protein Conformation Protein Folding SecB X-Ray Diffraction |
| title | Crystals of Acetylated SecB Diffract to 2.3-Å Resolution |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-09T08%3A26%3A24IST&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=Crystals%20of%20Acetylated%20SecB%20Diffract%20to%202.3-%C3%85%20Resolution&rft.jtitle=Journal%20of%20structural%20biology&rft.au=Dekker,%20Carien&rft.date=1999-12-30&rft.volume=128&rft.issue=3&rft.spage=237&rft.epage=242&rft.pages=237-242&rft.issn=1047-8477&rft.eissn=1095-8657&rft_id=info:doi/10.1006/jsbi.1999.4179&rft_dat=%3Cproquest_cross%3E69405028%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c255t-f9369d64ea97bb8da686ec493f8bf090b716473a5b86a0c48b52cbf63232c0393%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=69405028&rft_id=info:pmid/10633062&rfr_iscdi=true |