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Table 4 Data collection and refinement statistics* for Y74F and C298S mutants of E. coli Trpase.

From: Conformational changes and loose packing promote E. coli Tryptophanase cold lability

  Y74F [PDB:2V1P] C298S [pdb:2V0Y]
Data collection   
Space group F222 F222
Wavelength 1.5Å 1.5Å
Unit cell a = 118.7Å a = 120.5Å
  b = 120.2Å b = 118.8Å
  c = 171.7Å c = 171.5Å
  α = 90° α = 90°
  β = 90° β = 90°
  γ = 90° γ = 90°
Resolution 500.0-1.90 Å 500.0-1.98 Å
Highest resolution shell 1.97-1.90 Å 2. 05-1.98 Å
Total number of measured reflections
Total number of independent reflections
155,699
47,181
186,657
42,496
Completeness (%) 97.6% (97.8%) 99.3% (96.5%)
Rsym 0.054 (0.410) 0.117 (0.456)
I/σ (I) 19.0 (2.9) 12.7 (2.9)
Refinement   
Resolution range (Å) 6.0-1.9 8.0-2.0
R (%) 19.14 21.48
Rfree (%) 22.72 22.09
Protein atoms 3682 3678
Solvent atoms 595 519
Mg2+ atoms 1 1
Cl- atoms 1 1
RMS deviations from restraints target value   
Bond length (Å) 0.005 0.006
Bond Angle (°) 1.21 1.22
Average B factor
(for protein atoms) (Å2)
28.8 28.9
  1. Data in parenthesis correspond to the high resolution shell.