TABLE 1.
Data reduction and refinement statistics for MpTsdBA structure
| 142.65°-sweep data set (refinement) | Full 360° data set (Fe-SAD phasing) | |
|---|---|---|
| PDB code | 5LO9 | |
| Data collection | ||
| Synchrotron | ESRF (Grenoble, France) | |
| Beamline | ID-29 | |
| Wavelength (Å) | 1.7236 | |
| Space group | H32 | |
| Unit cell | ||
| a, b, c (Å) | 159.75, 159.75, 393.09 | 159.89, 159.89, 392.99 |
| α, β, γ (o) | 90.0, 90.0, 120.0 | |
| Resolution rangea (Å) | 113.13–2.75 (2.76–2.75) | 130.99–2.82 (2.83–2.82) |
| Total no. of reflections | 377,526 (2187) | 891,650 (6064) |
| No. of unique reflections | 50,199 (461) | 49,983 (442) |
| Completeness (%) | 99.0 (87.8) | 99.6 (94.2) |
| Anomalous completeness (%) | 98.7 (84.8) | 99.6 (94.1) |
| Multiplicity | 7.5 (4.7) | 19.0 (13.7) |
| Anomalous multiplicity | 3.9 (2.5) | 9.9 (7.0) |
| 〈I/σ(I)〉 | 14.9 (2.0) | 15.4 (2.4) |
| Rmeasb (%) | 11.7 (70.6) | 25.5 (184.7) |
| Rpim (%) | 5.7 (41.8) | 8.1 (69.2) |
| CC1/2c (%) | 99.7 (63.8) | 99.4 (75.7) |
| Refinement | ||
| Rcrystd (%) | 15.7 (25.9) | |
| Rfreee (%) | 19.8 (30.0) | |
| No. of non-H atoms | ||
| Protein | 7028 | |
| Ligands | 330 | |
| Waters | 113 | |
| r.m.s.d. bonds (Å) | 0.013 | |
| r.m.s.d. angles (°) | 1.50 | |
| Protein residues | Pro1–Leu191 and Arg237–Val515 (chain A), Pro1–Ala192 and Ala240–Ala516 (chain B) | |
| Ramachandran plot | ||
| Most favored (%) | 97.6 | |
| Allowed (%) | 2.4 | |
| Outliers (%) | 0 | |
| Rotamer outliers (%) | 0.9 | |
| Clashscore | 2.69 | |
| MolProbity scoref | 1.28 | |
| B-Factors (Å2) | ||
| Protein | 52.04 | |
| Ligands/ions | 50.43 | |
| Waters | 45.06 | |
a Information in parentheses refers to the last resolution shell.
b Rmeas = ΣhΣl|Ihl − 〈Ih〉|/ΣhΣl 〈Ih〉, where Ihl is the Ith observation of reflection h and 〈Ih〉.
c CC1/2 is as described previously (57).
d Rcryst = Σh‖Fobs(h)| − |Fcalc(h)‖/Σh|Fobs(h), where Fobs(h) − Fcalc(h) are the observed and calculated structure factors for reflection h, respectively.
e Rfree was calculated as Rfactor but using only 5% of reflections randomly selected and omitted from refinement.
f MolProbity score provides a single number that represents the central MolProbity protein quality statistics; it is a log-weighted combination of clashscore, Ramachandran not favored and bad side-chain rotamers, giving one number that reflects the crystallographic resolution at which those values would be expected.