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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.