Table 1.
Data collection and refinement statistics.
| Proteins | T4 lysozyme-MCU NTD S92E | T4 lysozyme-MCU NTD D119A |
|---|---|---|
| PDB ID: | 6JG0 | 6KVX |
| Data Collection | ||
| Space group | P65 | P65 |
| X-ray sourcea | PAL-5C | PAL-5C |
| Detector | ADSC Q315 | ADSC Q315 |
| Wavelength (Å) | 0.9795 | 0.9795 |
| Unit cell: a, b, c (Å) | 97.9, 97.9, 61.5 | 97.9, 97.9, 61.6 |
| Resolution range (Å)b | 50.0‒2.50 (2.54‒2.50) | 50.0‒2.85 (2.90‒2.85) |
| Rmergec | 8.3 (61.9) | 9.3 (59.1) |
| CC1/2d in outer shell (%) | 60.7 | 70.8 |
| I/σ(I) | 14.3 (3.0) | 12.3 (3.0) |
| Completeness (%) | 99.7 (99.8) | 98.7 (99.8) |
| Redundancy | 4.8 (3.5) | 4.2 (4.1) |
| Refinement | ||
| Resolution range (Å) | 42.5‒2.50 | 29.0‒2.85 |
| No. reflections | 11122 | 7489 |
| Rworke (%)/Rfree (%) | 19.0/26.0 | 18.0/26.2 |
| No. atoms/residues | ||
| Protein | 2011/253 | 2027/253 |
| SO42− | 10/2 | 20/4 |
| Water | 77 | − |
| B-factors (Å2) | ||
| Protein | 52.1 | 55.0 |
| SO42− | 88.6 | 81.9 |
| Water | 46.4 | − |
| Model statistics | ||
| rmsd bond length (Å) | 0.012 | 0.014 |
| rmsd bond angles (°) | 1.40 | 1.20 |
| Ramachandran plot (%) favoured/allowed/disallowed | 97.6/2.4/0.0 | 96.0/4.0/0.0 |
aBeamline 5 C at Pohang Acceleratory Laboratory (PAL) in South Korea.
bValues in parentheses are for highest-resolution shell.
cRmerge = ∑h ∑i │I(h)i − ‹I(h)›│/∑h ∑iI(h)i, where I(h) is the intensity of reflection of h, ∑h is the sum overall reflections and ∑i is the sum over i measurements of reflection h.
dCC1/2 in outer shell were calculated from HKL2000.
eRwork = Σhkl ||Fo | -|Fc ||/Σhkl | Fo | ; 5% of the reflections were excluded for the Rfree calculation.