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. Author manuscript; available in PMC: 2010 Mar 20.
Published in final edited form as: J Mol Biol. 2009 Jan 30;387(1):74–91. doi: 10.1016/j.jmb.2009.01.050

TABLE 1.

Crystallographic data for E. coli β148–152 mutant sliding clamp.

Beamline SSRL
Wavelength, Å 1.000

Resolution, Å 28.855 - 1.767

Space group P1

Temperature, K 100

Detector Mar325 CCD

Unit Cell parameters a = 40.838, b = 64.471, c = 72.111Å α = 73.83, β = 82.72, γ = 83.76°

Solvent content (%) 43.87

Unique reflections 59,193

I/σ(I) 23.3 (2.03)a

Average redundancy 1.8 (1.6)

Data completeness (%) 91.8 (80.8)

Mosacity (%) 2.0

Rmerge (%) 0.035 (0.347)

Refinement:
 R factor (%) 21.8
 Rfree (%)b 28.3
 Rmsd bond distance, Å 0.019
 Rmsd bond angle, ° 2.08
 Average B factors, Å2 35.3

Ramachandran Plot:
 Core, % 90.3
 Disallowed 0.8

No. of protein atoms 5,648

No. of solvent atoms 381

PDB code 3F1V
a

Values in parentheses refer to highest resolution shell 1.83-1.77 Å.

b

Rfree is calculated the same way as R factor for data omitted from refinement (5% of reflections for all data).