Table I. Data collection and refinement statistics.
| Data processing | |
| resolution(Å) | 30.0–2.40 (2.49–2.40) |
| No. of reflections | 13 721 (1364) |
| redundancy | 3.7 (3.7) |
| I/σI | 15.9 (3.5) |
| completeness (%) | 99.7 (100.0) |
| Rsym (%)a | 5.3 (40.1) |
| Refinement | |
| data range (Å) | 30.0–2.40 (2.55–2.40) |
| reflections in working set | 13 235 (1859) |
| reflections in Rfree set | 1358 (219) |
| Rcrys (%)b | 19.8 (24.9) |
| Rfree (%)c | 24.0 (29.3) |
| No. of protein atoms | 1925 |
| No. of ADP atoms | 27 |
| No. of Mg2+ atoms | 1 |
| No. of solvent atoms | 114 |
| r.m.s. deviation bond length (Å) | 0.007 |
| r.m.s. deviation bond angles (°) | 1.3 |
| average B-factor | 52.1 |
aRsym = ∑h′<|Ih – Ih′|>/∑h′Ih′ where <|Ih – Ih′|> is the average of the absolute deviation of a reflection Ih′ from the average Ih of its symmetry and Friedel equivalents.
bRcrys = ∑||Fo| – |Fc||/∑|Fo| where Fc is the calculated structure factor.
cRfree is as for Rcrys but calculated for 2% of randomly chosen reflections that were omitted from the refinement.