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. Author manuscript; available in PMC: 2013 Nov 13.
Published in final edited form as: Biochemistry. 2012 Oct 30;51(45):9234–9244. doi: 10.1021/bi301043k

Table 2.

Crystal data and refinement parameters

Parameter Dpo4 North Dpo4 South
X-ray source APS APS
Beamline ID24-E ID24-E
Detector ADSC Q315 ADSC Q315
Wavelength (Å) 0.979 0.979
Temperature (K) 110 110
No. of Crystals 1 1
Space group P21212 P21
Unit Cell (a, b, c; Å) 93.6,103.4,52.5 52.7,101.1,100.0
Resolution range (Å) 46.8–2.90 47.5–2.89
Highest resolution shella (3.00–2.90) (2.96–2.89)
No. of measurements 267168 262183
No. of unique reflections 11041 (1130) 21258 (1829)
Redundancy 3.6 (3.5) 3.2 (3.0)
Completeness (%) 97.8 (84.2) 96.0 (63.0)
R-mergeb (%) 8.8 (70.4) 14.0 (78.8)
Signal to noise (I/sI) 9.3 (1.9) 12.7 (1.8)
Model Composition
No. of amino acid residues 341 682
No. of water molecules 46 65
No. of Ca2+ ions 4 9
No. of template nucleotides 16 29
No. of primer nucleotides 14 26
No. of MC-dATP 1 2
Rfc (%) 20.2 20.6
R-freed (%) 27.6 26.5
Temperature factors
From Wilson plot (Å2) 75.1 60.8
r.m.s. standard deviation from ideal values
Bond lengths (Å) 0.008 0.010
Bond angles (°) 1.3 1.4
Dihedral angles (°) 20.6 20.8
a

Values in parentheses correspond to the highest resolution shells.

b

R-merge = ΣhklΣj=1,N|〈Ihkl〉−Ihkl,j|/ΣhklΣj=1,N|Ihkl,j|, where the outer sum (hkl) is taken over unique the reflections.

c

Rf= ΣhklFo,hkl|−k|Fc,hkl∥/Σhkl|Fo,hkl|, where |Fo,hkl| and |Fc,hkl| are the observed and calculated structure factors respectively.

d

Rfree idem, for the set of reflections (10% of the total) omitted from the refinement process.