Skip to main content

Table 1 X-ray data-collection and structure refinement statistics

From: Aldose reductase from Schistosoma japonicum: crystallization and structure-based inhibitor screening for discovering antischistosomal lead compounds

Data collection and processing
Processing software HKL2000
Synchrotron, beamline SSRF, BL17U
Wavelength (Å) 0.9791
Space group P21212
Unit cell parameters a, b, c (Å, °) a = 67.49, b = 91.00, c = 54.67
Resolution range (Å)1 30.0-2.20 (2.28-2.20)
Unique reflections 17617
Redundancy 6.4 (6.5)
Completeness (%) 99.8 (99.9)
Rmerge (%) 12.5 (37.1)
I/σ(I) 13.8 (5.0)
Refinement statistics
Refinement software PHENIX
Rwork (%)/Rfree(%)2 17.7/21.7
Average B factor, (Å2) 17.9
RMSD from ideal geometry, bonds (Å) 0.007
RMSD from ideal geometry, angles (°) 1.023
Protein atoms 2452
Water molecules 225
Residues in the Ramachandran plot
Most favored region (%) 92.5
Allowed region (%) 7.5
Generously allowed region (%) 0
Disallowed region (%) 0
  1. 1Values in parentheses are for the highest resolution shell.
  2. 2Rfree = ∑ Test ||Fobs| –|Fcalc||/∑Test |Fobs|, where “Test” is a test set of about 5% of the total reflections randomly chosen and set aside before refinement.