Table 1. Data collection and refinement statistics.
| Data set | Wild type |
| X-ray sourceSpace groupWavelength (Å)Resolution (Å)Total reflectionsUnique reflectionsAverage I/σ(I)RmergeaRedundancyCompleteness (%)b | 5C (SBII) at PALP650.9776050.0–2.40 (2.45–2.40)88,22515,41245.9 (5.7)0.25 (0.56)7.2 (7.5)99.6 (100) |
| Refinement | |
| Resolution range (Å)No. of reflections of working setNo. of reflections of test setNo. of amino acid residues | 27.4–2.424,77411,2591,312 |
| No. of water molecules | 20 |
| Rcryst bRfree cR.M.S. bond length (Å)R.M.S. bond angle (°)Average B value (Å2) (protein) | 0.170.200.0081.01057.9 |
| Average B value (Å2) (solvent) | 69.7 |
| Ramachandran plot | |
| Most favored (%) | 99.8 |
| Allowed (%) | 0.2 |
aRcryst = ∑|<I>−I|/∑<I>.
bRcryst = ∑| |Fo|−|Fc| |/∑|Fo|.
cRfree calculated with 5% of all reflections excluded from refinement stages using high-resolution data.Values in parentheses refer to the highest resolution shells.