Please use this identifier to cite or link to this item:
Title: Crystallization and preliminary X-ray characterization of the eukaryotic replication terminator Reb1-Ter DNA complex
Authors: Jaiswal, Rahul
Singh, Samarendra K.
Bastia, Deepak
Escalante, Carlos R.
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2015
Source: Jaiswal, R., Singh, S. K., Bastia, D., & Escalante, C. R. (2015). Crystallization and preliminary X-ray characterization of the eukaryotic replication terminator Reb1-Ter DNA complex. Acta crystallographica section F : structural biology communications, 71(4), 414-418.
Series/Report no.: Acta crystallographica section F : structural biology communications
Abstract: The Reb1 protein from Schizosaccharomyces pombe is a member of a family of proteins that control programmed replication termination and/or transcription termination in eukaryotic cells. These events occur at naturally occurring replication fork barriers (RFBs), where Reb1 binds to termination (Ter) DNA sites and coordinates the polar arrest of replication forks and transcription approaching in opposite directions. The Reb1 DNA-binding and replication-termination domain was expressed in Escherichia coli, purified and crystallized in complex with a 26-mer DNA Ter site. Batch crystallization under oil was required to produce crystals of good quality for data collection. Crystals grew in space group P21, with unit-cell parameters a = 68.9, b = 162.9, c = 71.1 Å, β = 94.7°. The crystals diffracted to a resolution of 3.0 Å. The crystals were mosaic and required two or three cycles of annealing. This study is the first to yield structural information about this important family of proteins and will provide insights into the mechanism of replication and transcription termination.
ISSN: 2053-230X
DOI: 10.1107/S2053230X15004112
Rights: © 2015 International Union of Crystallography. This paper was published in Acta Crystallographica Section F: Structural Biology Communications and is made available as an electronic reprint (preprint) with permission of International Union of Crystallography. The paper can be found at the following official DOI: [].  One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

Citations 20

Updated on Jan 29, 2023

Web of ScienceTM
Citations 20

Updated on Jan 28, 2023

Page view(s)

Updated on Jan 30, 2023

Download(s) 20

Updated on Jan 30, 2023

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.