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dc.contributor.authorJanson, C. A.en
dc.contributor.authorKonstantinidis, A. K.en
dc.contributor.authorLonsdale, J. T.en
dc.contributor.authorQiu, X.en
dc.rightsDefault Licence-
dc.subject3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/*chemistryen
dc.subjectBacterial Proteins/chemistryen
dc.subjectData Interpretation, Statisticalen
dc.subjectEscherichia coli/*enzymologyen
dc.subjectX-Ray Diffraction/methodsen
dc.titleCrystallization of Escherichia coli beta-ketoacyl-ACP synthase III and the use of a dry flash-cooling technique for data collectionen
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.abstractbeta-Ketoacyl-acyl carrier protein (ACP) synthase III (FabH) is a condensing enzyme active in the fatty-acid biosynthesis pathway of bacteria. The enzymes of this pathway provide a set of targets for the discovery of previously unknown antibiotics. FabH from Escherichia coli has been crystallized in two crystal forms using the sitting-drop vapor-diffusion technique. The first form crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 63.1, b = 65.1, c = 166.5 A; the second form crystallized in the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 72.7, c = 99.8 A. A flash-cooling technique using no cryoprotectant was utilized in obtaining data from the second type of crystals.en
heal.journalNameActa Crystallogr D Biol Crystallogren
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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