Table 3 X-ray data collection and refinement statistics
|  | WT SmBDH | SmBDH Q247A | SmBDH Q247A + V139Q |
|---|---|---|---|
Data collection | |||
 Space group | P43212 | P43212 | P43212 |
 Unit cell (Å, °) | a = b = 108.17, c = 82.88 α = β = γ = 90.00 | a = b = 108.68, c = 82.95 α = β = γ = 90.0 | a = b = 108.80, c = 83.11 α = β = γ = 90.0 |
 Wavelength (Å) | 1.54178 | 1.54178 | 1.54178 |
 Temperature (K) | 100 | 100 | 100 |
 Resolution (Å) | 25.0–2.0 (2.1–2.0) | 25.0–1.9 (2.0–1.9) | 25.0–1.8 (1.9–1.8) |
 Unique reflections | 33,823 (4496) | 39,724 (5531) | 46,796 (6911) |
 Rinta | 0.138 (0.689) | 0.109 (0.748) | 0.093 (0.793) |
 Average redundancy | 11.4 (8.8) | 17.3 (10.6) | 17.0 (12.5) |
 < I > / < σ(I) >  | 11.2 (2.0) | 18.7 (2.6) | 21.7 (1.9) |
 Completeness (%) | 100 (100) | 100 (100) | 100 (100) |
Refinement | |||
 R/Rfree | 0.162 (0.214)/0.279 (0.378) | 0.168 (0.340)/0.222 (0.347) | 0.160 (0.210)/0.295 (0.342) |
 Protein atoms | 3736 | 3792 | 3766 |
 Water molecules | 432 | 551 | 558 |
 Other atoms | 141 | 151 | 70 |
 r.m.s.d. from ideal bond lengthb (Å) | 0.010 | 0.009 | 0.010 |
 r.m.s.d. from ideal bond anglesb (°) | 1.497 | 1.486 | 1.612 |
 Wilson B-factor | 21.6 | 19.5 | 21.2 |
 Average B-factor for protein atoms (Å2) | 25.2 | 25.0 | 24.0 |
 Average B-factor for water molecules (Å2) | 33.0 | 32.6 | 33.1 |
Ramachandran plot statisticsc (%) | |||
 Allowed | 99.8 | 99.8 | 99.8 |
 Favored | 96.9 | 97.2 | 97.3 |
 Number of outliers | 1 | 1 | 1 |