X-ray Structure of Native Scorpion Toxin BmBKT×1 by Racemic Protein Crystallography Using Direct Methods.
The article offers information on a research conducted in order to determine the X-ray structure of native scorpion toxin BmBKTx1 using racemic protein crystallization. In BmBKTx1, racemic crystallization was used for the facile production of diffraction quality crystals. Racemic crystallography is...
| Publicado en: | Journal of the American Chemical Society Vol. 131; no. 4; pp. 1362 - 1364 |
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| Autores principales: | , , , , |
| Formato: | Artículo |
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American Chemical Society
2/4/2009
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| Materias: | |
| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=hlh&AN=36508540&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 36508540 longDbName: Humanities International Complete uiTag: AN controlInfo: bkinfo: jinfo: jid: 00027863 ACS jtl: Journal of the American Chemical Society issn: 00027863 maglogo: N pubinfo: dt: 2/4/2009 vid: 131 iid: 4 pid: 997 pub: American Chemical Society artinfo: ui: 36508540 10.1021/ja8077973 ppf: 1362 ppct: 2 formats: tig: atl: X-ray Structure of Native Scorpion Toxin BmBKT×1 by Racemic Protein Crystallography Using Direct Methods. aug: au: Mandal, Kalyaneswar Pentelute, Brad L. Tereshko, Valentina Kossiakoff, Anthony A. Kent, Stephen B. H. affil: Department of Chemistry, Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois 60637. Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois 60637. su: Toxins Crystallization Chemical structure Optical diffraction Crystals X-rays sug: subj: Toxins Crystallization Chemical structure Optical diffraction Crystals X-rays ab: The article offers information on a research conducted in order to determine the X-ray structure of native scorpion toxin BmBKTx1 using racemic protein crystallization. In BmBKTx1, racemic crystallization was used for the facile production of diffraction quality crystals. Racemic crystallography is stated to be a viable approach for obtaining structures of recalcitrant proteins. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2009 holdings: @attributes: islocal: N |
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