ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTCrystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxisAndrew J. Sharff, Lynn E. Rodseth, John C. Spurlino, and Florante A. QuiochoCite this: Biochemistry 1992, 31, 44, 10657–10663Publication Date (Print):November 1, 1992Publication History Published online1 May 2002Published inissue 1 November 1992https://pubs.acs.org/doi/10.1021/bi00159a003https://doi.org/10.1021/bi00159a003research-articleACS PublicationsRequest reuse permissionsArticle Views1349Altmetric-Citations396LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
MACROMOLECULES C-191 in hanging-drop with 20% PEGSOOO as precipitant.The typical crystal reaches 0.6 x 0.3 x 0.06mm in two weeks.The crystals belong to the orthorhombic space group P2 1 212 1 with unit cell dime1;;,ions of a= 46.1J\., b=86.9A and c=l26.5 A. Native datasets, with diffraction limit of 2.2 A. at both room temperature and low temperature, have been collected on a Rigaku it-axis.Molecular replacement using the MAP kinase ERK2 as a model structure and multiple isomorphous replacement have been applied to solve the structure.
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTRefined 1.8-.ANG. structure reveals the mode of binding of .beta.-cyclodextrin to the maltodextrin binding proteinAndrew J. Sharff, Lynn E. Rodseth, and Florante A. QuiochoCite this: Biochemistry 1993, 32, 40, 10553–10559Publication Date (Print):October 12, 1993Publication History Published online1 May 2002Published inissue 12 October 1993https://pubs.acs.org/doi/10.1021/bi00091a004https://doi.org/10.1021/bi00091a004research-articleACS PublicationsRequest reuse permissionsArticle Views696Altmetric-Citations148LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
