TABLE 1.
Data collection and refinement statistics
The numbers in parentheses refer to the highest resolution shell.
| apo | Man1P | GTP | GDP-Man | |
|---|---|---|---|---|
| Data collection | ||||
| Beamline | ID29 (ESRF) | Proxima1 (SOLEIL) | ID14-EH2 (ESRF) | ID14-EH4 (ESRF) |
| Resolution (Å) | 65.37-2.35 (2.48-2.35) | 65.21-2.10 (2.21-2.10) | 67.57-2.80 (2.95-2.80) | 50-2.70 (2.85-2.70) |
| Space group | P21 | P21 | P21 | C2221 |
| Cell dimension a, b, c (Å) | 64.01, 92.00, 69.69 | 63.93, 91.74, 69.73 | 65.93, 79.57, 70.95 | 84.23, 96.04, 217.12 |
| β (°) | 110.25 | 110.75 | 107.75 | |
| Unique reflections | 31,744 | 43,388 | 17,147 | 24,606 |
| Completeness (%) | 99.2 (96.9) | 98.7 (98.8) | 98.9 (99.1) | 99.8 (99.9) |
| Redundancy | 6.0 (5.4) | 3.1 (3.1) | 3.1 (3.1) | 5.7 (5.8) |
| <I/σI> | 23.5 (2.5) | 17.3 (2.5) | 16 (2.6) | 24.4 (4.2) |
| Rmerge (%)a | 5.5 (47) | 4.3 (47.1) | 6.1 (48) | 5.3 (43.7) |
| No molecules (arbitrary units) | 2 | 2 | 2 | 2 |
| Refinement | ||||
| Rcryst (%)b | 22.4 (36.8) | 18.70 (28.70) | 21.60 (32.10) | 19.11 (24.80) |
| Rfree (%)c | 27.3 (39.2) | 23.01 (31.70) | 26.97 (40.10) | 24.41 (29.80) |
| RMSDd | ||||
| Bond (Å) | 0.01 | 0.013 | 0.01 | 0.013 |
| Angles (°) | 1.154 | 1.335 | 1.218 | 1.457 |
| Number of atoms | ||||
| Proteine | 5365/5416 | 5456/5454 | 5420/5404 | 5421/5420 |
| Water/ions | 48/— | 162/7 | 20/2 | 38/1 |
| Ligands | — | 32 | 64 | 78 |
| Average B-factor (Å2) | ||||
| Protein | 76.03 | 50.53 | 75.18 | 64.08 |
| Water/ions | 47.16/— | 38.32/44.45 | 30.61/41.42 | 30.95/26.55 |
| Ligand | — | 49.6 | 56.25 | 42.95 |
| Ramachandran analysis | ||||
| Favored (%) | 97 | 97.6 | 95 | 97.3 |
| Outliers (%) | 0 | 0.2 | 0.2 | 0 |
| Protein Data Bank accession code | 2X5S | 2X65 | 2X60 | 2X5Z |
a Rmerge = Σhkl(Σi|Ihkl-〈Ihkl〉|)/Σhkl|〈Ihkl〉.
b Rcryst = Σhkl||Fo| − |Fc||/Σhkl|Fo|.
c Rfree is calculated for randomly selected reflections excluded from refinement.
d RMSD, root mean square deviation from ideal geometry.
e For each subunit in the dimer.