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

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INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X13034432

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资金

  1. Cancer Center Support Grant [P30CA036727]
  2. National Institute of General Medical Sciences (NIGMS) [R01 GM101167, R01 GM082923]
  3. Nebraska Department of Health and Human Services [LB506]
  4. NIGMS [P41 GM103403]
  5. US DOE [DE-AC02-06CH11357]

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Human primase synthesizes RNA primers and transfers them to the active site of Pol alpha 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 angstrom, alpha = 93.82, beta = 96.57, gamma = 111.72 degrees, and contained two heterodimers of full-length p49 and p59 subunits in the asymmetric unit.

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