TABLE 1.
Data collection and refinement statistics
I-SAD, iodine-based; MR, molecular replacement.
| Proteina |
|||
|---|---|---|---|
| MecA 121–218 | YpbH 104–194 | YpbH 101–194 | |
| Data collection | |||
| X-ray source | Rigaku FR-E | Rigaku MM-007HF | BL41XU, SPring-8 |
| Wavelength (Å) | 1.5418 | 1.5418 | 1.0000 |
| Space group | C2221 | P21 | I4122 |
| Unit cell (Å) | a = 69.52, b = 107.27, c = 109.61 | a = 28.93, b = 71.66, c = 39.33, β = 95.35 | a = 162.06, c = 142.85 |
| Number of molecules in ASU | 4 | 2 | 6 |
| Resolution (outer shell) (Å) | 2.17 (2.25-2.17) | 2.09 (2.21-2.09) | 2.4 (2.49-2.4) |
| Rmergeb (outer shell) (%) | 6.9 (43.1) | 7.9 (73.2) | 8.4 (78.2) |
| I/σ (outer shell) | 36.75 (4.55) | 9.09 (2.6) | 25.3 (3.0) |
| Completeness (outer shell) (%) | 99.4 (98.7) | 94.1 (88) | 99.7 (100) |
| Redundancy (outer shell) | 8.5 (7.9) | 2.9 (2.7) | 8.1 (8.3) |
| Wilson B factor (Å2) | 50.3 | 37.7 | 54.0 |
| Phasing protocol | I-SAD | I-SAD | MR |
| Refinement | |||
| R/Rfreec (%) | 22.2/27.9 | 21.8/30.4 | 23.0/27.0 |
| Number of atoms/B-factor: | |||
| Protein | 3063/51.3 | 1422/43.1 | 4332/50.0 |
| Water | 86/52.9 | 60/45.8 | 153/45.8 |
| Iodine | 35/69.1 | 14/62.0 | |
| All | 3184/51.5 | 1496/43.4 | 4485/49.8 |
| Ramachandran plot | |||
| Most favored (%) | 86.6 | 91.0 | 89.1 |
| Additional allowed (%) | 11.4 | 9.0 | 10.9 |
| Generously allowed (%) | 0.9 | 0.0 | 0.0 |
| Disallowed (%) | 1.1 | 0.0 | 0.0 |
| r.m.s.d. | |||
| Bond distances (Å) | 0.01 | 0.01 | 0.007 |
| Bond angles (°) | 1.31 | 1.16 | 1.161 |
| Omega values (°) | 1.103 | 0.858 | 1.034 |
aValues in parentheses are for the highest resolution shell.
bRmerge = ΣhΣi|Ih,i − Ih|/ΣhΣiIh,i, where Ih is the mean intensity of the i observations of symmetry related reflections of h.
c R = Σ|Fobs − Fcalc|/ΣFobs, where Fcalc is the calculated protein structure factor from the atomic model. Rfree was calculated with 5% of the reflections selected randomly.