Table 1.
Data collection and refinement statistics
| Data set | |
| Beamline | APS, 19-BM |
| Wavelength (Å) | 0.9794 |
| Space group | P21 |
| a,b,c (Å) | 53.06, 56.57, 112.65 |
| β (°) | 95.65 |
| Resolution (Å) | 30–2.0 |
| (2.02–2.09) | |
| No. observations/ | 3,37,222 |
| No. unique reflections | 87,860 |
| Completeness (%) | 99.6 (99.5) |
| Redundancy | 3.8 (3.5) |
| Rmarge (%)a | 11.0 (30.0) |
| I/σb | 11.9 (3.1) |
| Refinement | |
| Protein molecules | 3 |
| Solvent/Mg ions | 674/3 |
| Rcryst (%)c | 16.70 |
| Rfree (%)d | 20.30 |
| RMSD bonds (Å) | 0.009 |
| RMSD angles (°) | 1.158 |
| RMSD chiral centers | 0.078 |
| B average protein/water (Å2) | 35.3/39.6 |
| Ramachandran plot (%)e favored/allowed/outlierse | 95.7/100/0 |
Values in parentheses indicate values for the highest resolution shell
a
Rsym = (Σ|Ihkl − <I>|)/ΣIhkl, where the average intensity <I> is taken over all symmetry equivalent measurements and Ihkl is the measured intensity for any given reflection.
b
I/σ is the mean reflection intensity divided by the average estimated error.
c
Rcryst = ||Fo| − |Fc||/|Fo|, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.
d
Rfree is equivalent to Rcryst but is calculated for 5% of the reflections chosen at random and omitted from the refinement process. r.m.s.d., root mean square deviation.
e
Validated using MolProbity server [17]