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Crystallization and preliminary X-ray diffraction analysis of motif N from Saccharomyces cerevisiae Dbf4.
- 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.
- Subjects :
- Amino Acid Motifs
Amino Acid Sequence
Cell Cycle Proteins isolation & purification
Crystallization
Crystallography, X-Ray
Molecular Sequence Data
Protein Structure, Tertiary
Saccharomyces cerevisiae Proteins isolation & purification
Cell Cycle Proteins chemistry
Saccharomyces cerevisiae chemistry
Saccharomyces cerevisiae Proteins chemistry
X-Ray Diffraction
Subjects
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