Table 3.
Crystal structure data collection and refinement statistics
| Statistic(s) | MatB | MatB-ATP |
|---|---|---|
| Data collection | ||
| Space group | P21 | P61 |
| Cell dimensions | ||
| a,b,c (Å) | 133.9, 58.8, 139.0 | 173.1, 173.1, 47.7 |
| a, b, g (°) | 90, 91.7, 90 | 90, 90, 120 |
| Wavelength | 0.98 | 0.98 |
| Resolution (Å)a | 25–1.7 (1.74–1.7) | 25–2.0 (2.03–2.0) |
| Rmergea | 7.6 (48.3) | 4.7 (45.4) |
| I/σIa | 16.8 (3.5) | 31.4 (7.3) |
| Completeness (%)a | 97.1 (95.5) | 99.5 (100) |
| Redundancya | 4.2 (3.8) | 12.5 (10.8) |
| Refinement | ||
| Resolution (Å)a | 25–1.7 (1.74–1.7) | 25–2.0 (2.03–2.0) |
| No. of reflectionsb | 225,397 (11,309) | 53,454 (2,718) |
| Rwork/Rfreec | 0.16/0.20 | 0.16/0.20 |
| No. of atoms | ||
| Protein | 15,413 | 3,927 |
| Water | 2,607 | 619 |
| Average B-factor (Å2) | 17.6 | 26.7 |
| Ramachandran (%) | ||
| Most favored | 98.9 | 99.2 |
| Allowed | 1.1 | 0.8 |
| Disallowed | 0 | 0 |
| RMSDs | ||
| Bond lengths (Å) | 0.006 | 0.007 |
| Bond angles (°) | 1.008 | 1.052 |
| PDB accession no. | 4FUQ | 4FUT |
a
Data in parentheses represent highest resolution shell.
b
Data in parentheses represent the number of reflections used during refinement.
c
Rfactor is determined as Rfactor = ∑|Fobs − Fcalc|/∑|Fobs|, where Rwork refers to the Rfactor for the data utilized in the refinement, Rfree refers to the Rfactor for 5% of the data that were excluded from the refinement, Fobs refers to the observed structure factor amplitude, and Fcalc refers to the calculated structure amplitude from the corresponding model.