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

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

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)206-210
Number of pages5
JournalActa Crystallographica Section F:Structural Biology Communications
Issue number2
StatePublished - Feb 2014


  • DNA replication
  • human DNA primase
  • p49 subunit
  • p58 subunit

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


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