Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase

Recombinant Brassica oleracea histidinol dehydrogenase (HDH) has been crystallized in various space groups using the method of vapour diffusion. The presence or absence of inhibitors and substrates as well as the use of different precipitants has enabled the growth of five different crystal forms. E...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1996-11, Vol.52 (6), p.1188-1190
Hauptverfasser: Cowan-Jacob, S. W., Rahuel, J., Nagai, A., Iwasaki, G., Ohta, D.
Format: Artikel
Sprache:eng
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 1190
container_issue 6
container_start_page 1188
container_title Acta crystallographica. Section D, Biological crystallography.
container_volume 52
creator Cowan-Jacob, S. W.
Rahuel, J.
Nagai, A.
Iwasaki, G.
Ohta, D.
description Recombinant Brassica oleracea histidinol dehydrogenase (HDH) has been crystallized in various space groups using the method of vapour diffusion. The presence or absence of inhibitors and substrates as well as the use of different precipitants has enabled the growth of five different crystal forms. Extensive searches with the first crystal form (A) failed to produce any useful heavy‐atom derivatives, mainly because of the instability of the crystals. This provoked the search for further crystal forms in the hope of finding more suitable crystals. At least two of these crystal forms are of interest for further study.
doi_str_mv 10.1107/S0907444996008396
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_77918975</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>77918975</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3368-b3adc1bc335d34f1a8994f4f2f5096f02ba28896d144bbed6811202ab7c1649c3</originalsourceid><addsrcrecordid>eNqFkN1LG0EUxYdSaTT2D-hL2ae-rc7XzsdjSG0URTEqoYIM87XJ6GQ3nUnQ7V_vSkIr9KFP9x7u7xy4B4AvCB4hBPnxDZSQU0qlZBAKItkHsI-IlCWElH98tw_AQc6PEEKMCf8EBqjCUlYC74OHceryWscYfut1aJtCN65YJR_DMjQ6dYXd3dt50qtFsD2gY5dDLtq6sNoYPffFIuR1cKFpY-H8onOpnftGZ38I9mods_-8m0Nw9-PkdnxaXlxNzsaji9ISwkRpiHYWmV5UjtAaaSElrWmN6wpKVkNsNBZCMocoNcY7JhDCEGvDLWJUWjIE37a5q9T-2vi8VsuQrY9RN77dZMW5RELyqgfRFrSpzTn5Wq1SWPZ_KgTVW6fqn057z9dd-MYsvfvr2JXYA2ILPIfou_8nqtHP75MpZL0YgnJr7Qv0L3-sOj0pxgmv1OxyosbnBF-fTu_VjLwCn4SS-Q</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>77918975</pqid></control><display><type>article</type><title>Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase</title><source>Crystallography Journals Online</source><creator>Cowan-Jacob, S. W. ; Rahuel, J. ; Nagai, A. ; Iwasaki, G. ; Ohta, D.</creator><creatorcontrib>Cowan-Jacob, S. W. ; Rahuel, J. ; Nagai, A. ; Iwasaki, G. ; Ohta, D.</creatorcontrib><description>Recombinant Brassica oleracea histidinol dehydrogenase (HDH) has been crystallized in various space groups using the method of vapour diffusion. The presence or absence of inhibitors and substrates as well as the use of different precipitants has enabled the growth of five different crystal forms. Extensive searches with the first crystal form (A) failed to produce any useful heavy‐atom derivatives, mainly because of the instability of the crystals. This provoked the search for further crystal forms in the hope of finding more suitable crystals. At least two of these crystal forms are of interest for further study.</description><identifier>ISSN: 1399-0047</identifier><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><identifier>DOI: 10.1107/S0907444996008396</identifier><identifier>PMID: 15299582</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><ispartof>Acta crystallographica. Section D, Biological crystallography., 1996-11, Vol.52 (6), p.1188-1190</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,3987,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15299582$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cowan-Jacob, S. W.</creatorcontrib><creatorcontrib>Rahuel, J.</creatorcontrib><creatorcontrib>Nagai, A.</creatorcontrib><creatorcontrib>Iwasaki, G.</creatorcontrib><creatorcontrib>Ohta, D.</creatorcontrib><title>Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase</title><title>Acta crystallographica. Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>Recombinant Brassica oleracea histidinol dehydrogenase (HDH) has been crystallized in various space groups using the method of vapour diffusion. The presence or absence of inhibitors and substrates as well as the use of different precipitants has enabled the growth of five different crystal forms. Extensive searches with the first crystal form (A) failed to produce any useful heavy‐atom derivatives, mainly because of the instability of the crystals. This provoked the search for further crystal forms in the hope of finding more suitable crystals. At least two of these crystal forms are of interest for further study.</description><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNqFkN1LG0EUxYdSaTT2D-hL2ae-rc7XzsdjSG0URTEqoYIM87XJ6GQ3nUnQ7V_vSkIr9KFP9x7u7xy4B4AvCB4hBPnxDZSQU0qlZBAKItkHsI-IlCWElH98tw_AQc6PEEKMCf8EBqjCUlYC74OHceryWscYfut1aJtCN65YJR_DMjQ6dYXd3dt50qtFsD2gY5dDLtq6sNoYPffFIuR1cKFpY-H8onOpnftGZ38I9mods_-8m0Nw9-PkdnxaXlxNzsaji9ISwkRpiHYWmV5UjtAaaSElrWmN6wpKVkNsNBZCMocoNcY7JhDCEGvDLWJUWjIE37a5q9T-2vi8VsuQrY9RN77dZMW5RELyqgfRFrSpzTn5Wq1SWPZ_KgTVW6fqn057z9dd-MYsvfvr2JXYA2ILPIfou_8nqtHP75MpZL0YgnJr7Qv0L3-sOj0pxgmv1OxyosbnBF-fTu_VjLwCn4SS-Q</recordid><startdate>199611</startdate><enddate>199611</enddate><creator>Cowan-Jacob, S. W.</creator><creator>Rahuel, J.</creator><creator>Nagai, A.</creator><creator>Iwasaki, G.</creator><creator>Ohta, D.</creator><general>International Union of Crystallography</general><scope>BSCLL</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199611</creationdate><title>Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase</title><author>Cowan-Jacob, S. W. ; Rahuel, J. ; Nagai, A. ; Iwasaki, G. ; Ohta, D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3368-b3adc1bc335d34f1a8994f4f2f5096f02ba28896d144bbed6811202ab7c1649c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cowan-Jacob, S. W.</creatorcontrib><creatorcontrib>Rahuel, J.</creatorcontrib><creatorcontrib>Nagai, A.</creatorcontrib><creatorcontrib>Iwasaki, G.</creatorcontrib><creatorcontrib>Ohta, D.</creatorcontrib><collection>Istex</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cowan-Jacob, S. W.</au><au>Rahuel, J.</au><au>Nagai, A.</au><au>Iwasaki, G.</au><au>Ohta, D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>1996-11</date><risdate>1996</risdate><volume>52</volume><issue>6</issue><spage>1188</spage><epage>1190</epage><pages>1188-1190</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>Recombinant Brassica oleracea histidinol dehydrogenase (HDH) has been crystallized in various space groups using the method of vapour diffusion. The presence or absence of inhibitors and substrates as well as the use of different precipitants has enabled the growth of five different crystal forms. Extensive searches with the first crystal form (A) failed to produce any useful heavy‐atom derivatives, mainly because of the instability of the crystals. This provoked the search for further crystal forms in the hope of finding more suitable crystals. At least two of these crystal forms are of interest for further study.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>15299582</pmid><doi>10.1107/S0907444996008396</doi><tpages>3</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1399-0047
ispartof Acta crystallographica. Section D, Biological crystallography., 1996-11, Vol.52 (6), p.1188-1190
issn 1399-0047
0907-4449
1399-0047
language eng
recordid cdi_proquest_miscellaneous_77918975
source Crystallography Journals Online
title Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T16%3A29%3A15IST&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=Crystallization%20and%20preliminary%20crystallographic%20analysis%20of%20cabbage%20histidinol%20dehydrogenase&rft.jtitle=Acta%20crystallographica.%20Section%20D,%20Biological%20crystallography.&rft.au=Cowan-Jacob,%20S.%20W.&rft.date=1996-11&rft.volume=52&rft.issue=6&rft.spage=1188&rft.epage=1190&rft.pages=1188-1190&rft.issn=1399-0047&rft.eissn=1399-0047&rft_id=info:doi/10.1107/S0907444996008396&rft_dat=%3Cproquest_cross%3E77918975%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=77918975&rft_id=info:pmid/15299582&rfr_iscdi=true