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Table 2 X-ray data collection and refinement statistics

From: Crystal structure of signal regulatory protein gamma (SIRPγ) in complex with an antibody Fab fragment

Data collection  
 X-ray source Diamond I03
 Wavelength (Å) 0.97630
 Space group P 21212
 Unit cell (Å) a = 140.4, b = 174.2, c = 81.7
 Resolution range (Å) 30.0 – 2.50 (2.59-2.50)
 Unique reflections 71197 (7000)
 Completeness (%) 100 (100)
 Redundancy 12.3 (10.5)
 Average I/σI 14.9 (2.1)
 Rmerge 0.157 (−−)
Refinement  
 Resolution range (Å) 30.0 – 2.50
 No. of atoms (protein/other atoms) 11212/323
 Rms bond length deviation (Å) 0.008
 Rms bond angle deviation (°) 1.2
 Mean B-factor (protein/other atoms[Å2]) 38/54
 Residues in preferred regions (%) 1112 (89.5)
 Residues in allowed regions (%) 128 (10.3)
 Residues in disallowed regions (%) 3 (0.2)
  1. aRwork and Rfree are defined by R = Σ hkl ||F obs | − |F calc ||/Σ hkl|Fobs|, where h, k, l are the indices of the reflections (used in refinement for Rwork; 5%, not used in refinement, for Rfree), Fobs and Fcalc are the structure factors, deduced from measured intensities and calculated from the model, respectively.