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Crystallization and preliminary X-ray diffraction analysis of motif N from Saccharomyces cerevisiae Dbf4.

Authors :
Matthews LA
Duong A
Prasad AA
Duncker BP
Guarné A
Source :
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2009 Sep 01; Vol. 65 (Pt 9), pp. 890-4. Date of Electronic Publication: 2009 Aug 22.
Publication Year :
2009

Abstract

The Cdc7-Dbf4 complex plays an instrumental role in the initiation of DNA replication and is a target of replication-checkpoint responses in Saccharomyces cerevisiae. Cdc7 is a conserved serine/threonine kinase whose activity depends on association with its regulatory subunit, Dbf4. A conserved sequence near the N-terminus of Dbf4 (motif N) is necessary for the interaction of Cdc7-Dbf4 with the checkpoint kinase Rad53. To understand the role of the Cdc7-Dbf4 complex in checkpoint responses, a fragment of Saccharomyces cerevisiae Dbf4 encompassing motif N was isolated, overproduced and crystallized. A complete native data set was collected at 100 K from crystals that diffracted X-rays to 2.75 A resolution and structure determination is currently under way.

Details

Language :
English
ISSN :
1744-3091
Volume :
65
Issue :
Pt 9
Database :
MEDLINE
Journal :
Acta crystallographica. Section F, Structural biology and crystallization communications
Publication Type :
Academic Journal
Accession number :
19724125
Full Text :
https://doi.org/10.1107/S1744309109029376