Journal article
Overexpression, Purification, and Crystallization of the DNA Binding and Dimerization Domains of the Epstein-Barr Virus Nuclear Antigen 1 (∗)
Abstract
The Epstein-Barr virus nuclear antigen (EBNA) 1 binds to and activates DNA replication from the latent origin of Epstein-Barr virus. Six different fragments of EBNA1 that retain DNA binding activity were expressed in bacteria, purified, and crystallized. Two fragments, EBNA470-619 and EBNA470-607, formed well ordered crystals that diffracted beyond 2.5-A resolution. Two different EBNA470-619 crystals were grown from sodium formate, pH 6-6.5. …
Authors
Barwell JA; Bochkarev A; Pfuetzner RA; Tong H; Yang DSC; Frappier L; Edwards AM
Journal
Journal of Biological Chemistry, Vol. 270, No. 35, pp. 20556–20559
Publisher
Elsevier
Publication Date
September 1995
DOI
10.1074/jbc.270.35.20556
ISSN
0021-9258
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Antigens, ViralBase SequenceChromatography, DEAE-CelluloseCloning, MolecularCrystallizationDNA PrimersDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelEpstein-Barr Virus Nuclear AntigensEscherichia coliGenetic VectorsHerpesvirus 4, HumanMolecular Sequence DataPolymerase Chain ReactionRecombinant ProteinsRestriction MappingThermodynamics