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. 2019 May 3;3(9):1450–1459. doi: 10.1182/bloodadvances.2018027011

Table 1.

Crystallographic data collection and refinement statistics

Sample Mouse GP1bαN Mouse Mac-1 I
Data collection
 Space group P212121 P41212
 Cell dimensions
  a, b, c (Å) 61.5, 72.8, 164.0 62.9, 62.9, 336.2
  α, β, γ (°) 90.0, 90.0, 90.0 90.0, 90.0, 90.0
 Resolution, Å 29.9-2.0 45.9-2.5
 Rmerge* 11.1 12.5
 I/σI; CC(1/2) 7.0 (1.9); 0.997 (0.78) 8.2 (1.5); 0.903 (0.68)
 Completeness (%) 99.0 (90.0) 86.7 (67.2)
 Redundancy 4.3 (1.3) 6.2 (2.5)
Refinement
 Number of reflections 48095 21236
 Rwork/Rfree 0.192/0.237 0.222/0.271
 B factors, Å2
  Protein 29.8 48.2
 RMS deviations
  Bond lengths, Å 0.018 0.021
  Bond angles, ° 1.96 1.85

RMS, root mean square.

*

Rmerge = Sum(h) [Sum(j) [I(hj) − <Ih>]/Sum(hj) <Ih>, where I is the observed intensity and <Ih> is the average intensity of multiple observations from symmetry-related reflections calculated with SCALA.

Values in parentheses are for the highest resolution shell.

Rwork = Sum(h) ||Fo|h − |Fc|h| / Sum(h)|Fo|h, where Fo and Fc are the observed and calculated structure factors, respectively. Rfree computed as in Rwork, but only for 5% randomly selected reflections, which were omitted in refinement, calculated using REFMAC.