publication . Article . 2017

Structure of the family B DNA polymerase from the hyperthermophilic archaeon Pyrobaculum calidifontis.

Jingxu Guo; Wenling Zhang; Alun R. Coker; Steve P. Wood; Jonathan B. Cooper; Shazeel Ahmad; Syed Ali; Naeem Rashid; Muhummad Akhtar;
Open Access
  • Published: 26 Apr 2017
  • Publisher: INT UNION CRYSTALLOGRAPHY
  • Country: United Kingdom
Abstract
<jats:p>The family B DNA polymerase from<jats:italic>Pyrobaculum calidifontis</jats:italic>(<jats:italic>Pc</jats:italic>-polymerase) consists of 783 amino acids and is magnesium-ion dependent. It has an optimal pH of 8.5, an optimal temperature of 75°C and a half-life of 4.5 h at 95°C, giving it greater thermostability than the widely used<jats:italic>Taq</jats:italic>DNA polymerase. The enzyme is also capable of PCR-amplifying larger DNA fragments of up to 7.5 kb in length. It was shown to have functional, error-correcting 3′–5′ exonuclease activity, as do the related high-fidelity DNA polymerases from<jats:italic>Pyrococcus furiosus</jats:italic>,<jats:italic...
Subjects
free text keywords: Science & Technology, Life Sciences & Biomedicine, Physical Sciences, Biochemical Research Methods, Biochemistry & Molecular Biology, Biophysics, Crystallography, DNA polymerase, Pc-polymerase, protein crystallography, protein structure, molecular replacement, refinement, Pyrobaculum calidifontis, CRYSTAL-STRUCTURE, WEB SERVER, INSIGHTS, Exonuclease, biology.protein, biology, Polymerase, Pyrococcus furiosus, biology.organism_classification, Chemistry, Pyrobaculum, Stereochemistry, DNA, chemistry.chemical_compound, DNA polymerase, Processivity, Thermococcus kodakarensis
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publication . Article . 2017

Structure of the family B DNA polymerase from the hyperthermophilic archaeon Pyrobaculum calidifontis.

Jingxu Guo; Wenling Zhang; Alun R. Coker; Steve P. Wood; Jonathan B. Cooper; Shazeel Ahmad; Syed Ali; Naeem Rashid; Muhummad Akhtar;