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Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1570-4. doi: 10.1107/S2053230X14019906. Epub 2014 Oct 25.

Crystallization, room-temperature X-ray diffraction and preliminary analysis of Kaposi's sarcoma herpesvirus LANA bound to DNA.

Author information

1
Department of Structural Biology, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124 Braunschweig, Germany.
2
Institute of Virology, Hannover Medical School, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany.

Abstract

The 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.

KEYWORDS:

Kaposi's sarcoma herpesvirus; latency-associated nuclear antigen; structure-guided mutagenesis

PMID:
25372834
PMCID:
PMC4231869
DOI:
10.1107/S2053230X14019906
[Indexed for MEDLINE]
Free PMC Article

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