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dc.contributor.authorHellert, Jan
dc.contributor.authorKrausze, Joern
dc.contributor.authorSchulz, Thomas F
dc.contributor.authorLührs, Thorsten
dc.date.accessioned2015-07-31T14:30:59Zen
dc.date.available2015-07-31T14:30:59Zen
dc.date.issued2014-11en
dc.identifier.citationCrystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA. 2014, 70 (Pt 11):1570-4 Acta Crystallogr F Struct Biol Communen
dc.identifier.issn2053-230Xen
dc.identifier.pmid25372834en
dc.identifier.doi10.1107/S2053230X14019906en
dc.identifier.urihttp://hdl.handle.net/10033/561317en
dc.description.abstractThe latency-associated nuclear antigen (LANA) is the latent origin-binding protein and chromatin anchor of the Kaposi's sarcoma herpesvirus (KSHV/HHV-8) genome. Its C-terminal domain (CTD) binds sequence-specifically to the viral origin of replication, whereas the N-terminal domain links it to nucleosomes of cellular chromatin for long-term persistence in dividing host cells. Here, the crystallization and X-ray data acquisition of a mutant LANA CTD in complex with its wild-type target DNA LBS1 is described. This report describes the rational protein engineering for successful co-crystallization with DNA and X-ray diffraction data collection at room temperature on the high-brilliance third-generation synchrotron PETRA III at DESY, Germany.
dc.language.isoenen
dc.subject.meshAntigens, Viralen
dc.subject.meshCrystallizationen
dc.subject.meshDNA, Viralen
dc.subject.meshHerpesvirus 8, Humanen
dc.subject.meshNuclear Proteinsen
dc.subject.meshProtein Structure, Secondaryen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshSarcoma, Kaposien
dc.subject.meshX-Ray Diffractionen
dc.titleCrystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany.en
dc.identifier.journalActa crystallographica. Section F, Structural biology communicationsen
refterms.dateFOA2018-06-13T01:29:04Z
html.description.abstractThe latency-associated nuclear antigen (LANA) is the latent origin-binding protein and chromatin anchor of the Kaposi's sarcoma herpesvirus (KSHV/HHV-8) genome. Its C-terminal domain (CTD) binds sequence-specifically to the viral origin of replication, whereas the N-terminal domain links it to nucleosomes of cellular chromatin for long-term persistence in dividing host cells. Here, the crystallization and X-ray data acquisition of a mutant LANA CTD in complex with its wild-type target DNA LBS1 is described. This report describes the rational protein engineering for successful co-crystallization with DNA and X-ray diffraction data collection at room temperature on the high-brilliance third-generation synchrotron PETRA III at DESY, Germany.


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