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Crystallization and preliminary X-ray diffraction analysis of human DNA primase

Authors :
Yoshiaki Suwa
Nigar D. Babayeva
Tahir H. Tahirov
Jianyou Gu
Andrey G. Baranovskiy
Vinod B. Agarkar
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.

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