Table 1. Data collection and refinement statistics (molecular replacement)
ScV1 MgScV1 Sra
Data collection
Space groupC 1 2 1C 1 2 1
Cell dimensions
 a, b, c (Å)468.48, 159.74, 245.04468.02, 159.65, 248.27
 α, β, γ (°)90.00, 113.88, 90.0090.00, 113.75, 90.00
Resolution (Å)40.1–7.0 (7.249–7.0)b39.72–6.211 (6.432–6.211)
R merge 0.2558 (2.076)0.2321 (3.223)
I/σI7.82 (1.41)12.01 (0.88)c
Completeness (%)99.0 (94.0)88.0d
Redundancy8.5 (8.4)11.1 (11.5)
CC 1/20.988 (0.366)0.983 (0.377)
CC*0.997 (0.732)0.996 (0.740)
Refinement
Resolution (Å)40.1–7.039.72–6.211
No. reflections26,08733,464
Rwork/Rfree26.04/30.925.45/30.18
No. atoms
 Protein44,76047,363
 Ligand/ion00
 Water00
B‐factors
 Protein291320
Rms deviations
 Bond lengths (Å)0.0010.002
 Bond angles (°)0.420.62
  • a Two crystals.

  • b Values in parentheses are for highest resolution shell.

  • c I/σI in the highest resolution shell after elliptical truncation = 1.51.

  • d See Appendix Table S1.