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Literature summary for 2.7.7.B16 extracted from

  • Ito, N.; Nureki, O.; Shirouzu, M.; Yokoyama, S.; Hanaoka, F.
    Crystallization and preliminary X-ray analysis of a DNA primase from hyperthermophilic archaeon Pyrococcus horikoshii (2001), J. Biochem., 130, 727-730.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli as a fusion protein with a hexa-histidine tag Pyrococcus horikoshii

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method at 20°C, with polyethylene glycol 8000 as the precipitant. The crystals belong to the P3(2)21 with unit-cell parameters a = b = 77.8, c = 129.6 A, and alpha = beta = 90°, gamma = 120°. Crystals of the selenomethionine derivative are obtained by means of a cross-seeding method using native crystals. The data for the native and selenomethionine-substituted crystals are collected to 1.8 and 2.2 A resolution Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O57934 and O57935 O57934: small subunit, O57935: large subunit
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Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus horikoshii

General Information

General Information Comment Organism
physiological function at the initiation of chromosomal DNA replication, DNA primases synthesize short RNA primers, which are subsequently elongated by DNA polymerases Pyrococcus horikoshii