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Crystallization and preliminary X-ray diffraction analysis of human DNA primase
- Source :
- Acta Crystallographica Section F Structural Biology Communications. 70:206-210
- Publication Year :
- 2014
- Publisher :
- International Union of Crystallography (IUCr), 2014.
-
Abstract
- Human primase synthesizes RNA primers and transfers them to the active site of Pol α with subsequent extension with dNTPs. Human primase is a heterodimer of two subunits: a small catalytic subunit (p49) and a large subunit (p58). The structural details of the initiation and elongation steps of primer synthesis, as well as primer length counting, are not known. To address these questions, structural studies of human primase were initiated. Two types of crystals were obtained. The best diffracting crystals belonged to space group P1, with unit-cell parameters a = 86.2, b = 88.9, c = 94.68 Å, α = 93.82, β = 96.57, γ = 111.72°, and contained two heterodimers of full-length p49 and p59 subunits in the asymmetric unit.
- Subjects :
- Protein Conformation
Protein subunit
Biophysics
DNA replication
Active site
DNA Primase
Biology
Crystallography, X-Ray
Condensed Matter Physics
Biochemistry
Crystallography
chemistry.chemical_compound
Protein structure
chemistry
Crystallization Communications
Structural Biology
Genetics
biology.protein
Humans
Electrophoresis, Polyacrylamide Gel
Primase
Elongation
Primer (molecular biology)
Crystallization
DNA
Subjects
Details
- ISSN :
- 2053230X
- Volume :
- 70
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section F Structural Biology Communications
- Accession number :
- edsair.doi.dedup.....c56a1f81bb49b7608b843ebc51e5f044
- Full Text :
- https://doi.org/10.1107/s2053230x13034432