Table 1.

Crystallographic data collection and refinement statistics

SampleMouse GP1bαNMouse Mac-1 I
Data collection
 Space groupP212121P41212
 Cell dimensions
  a, b, c (Å)61.5, 72.8, 164.062.9, 62.9, 336.2
  α, β, γ (°)90.0, 90.0, 90.090.0, 90.0, 90.0
 Resolution, Å29.9-2.045.9-2.5
 Rmerge*11.112.5
 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)
 Redundancy4.3 (1.3)6.2 (2.5)
Refinement
 Number of reflections4809521236
 Rwork/Rfree0.192/0.2370.222/0.271
 B factors, Å2
  Protein29.848.2
 RMS deviations
  Bond lengths, Å0.0180.021
  Bond angles, °1.961.85
  • 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.