Table 1.
T4 lysozyme‐MCU NTD | T4 lysozyme‐MCU NTD S92A | MCU NTD‐E | |
---|---|---|---|
PDB ID: 4XSJ | PDB ID: 5BZ6 | PDB ID: 4XTB | |
Data collection | |||
Space groupa | P65 | P65 | P65 |
X‐ray sourceb and detector | PAL‐5C ADSC Q315r | PAL‐5C ADSC Q315r | PAL‐7A ADSC Q270 |
Wavelength (Å) | 0.9795 | 0.9795 | 0.9793 |
Unit cell: a, b, c (Å) | 98.1, 98.1, 62.4 | 97.8, 97.8, 61.5 | 55.5, 55.5, 68.9 |
α, β, γ (°) | 90.0, 90.0, 120.0 | 90.0, 90.0, 120.0 | 90.0, 90.0, 120.0 |
Resolution range (Å)c | 50–1.80 (1.83–1.80) | 50–2.75 (2.80–2.75) | 50−1.50 (1.53−1.50) |
R merge d | 6.8 (54.6) | 12.3 (56.3) | 4.7 (51.5) |
I/σI | 18.2 (3.2) | 6.8 (3.3) | 11.9 (3.6) |
Completeness (%) | 99.5 (98.3) | 99.5 (100.0) | 99.4 (100.0) |
Redundancy | 8.0 (6.3) | 4.7 (5.3) | 5.7 (5.6) |
Refinement | |||
Resolution range (Å)c | 48.5–1.80 | 34.9–2.75 | 48.0–1.50 |
No. reflections | 29581 | 8147 | 17594 |
R work e (%)/R free (%) | 12.7/19.0 | 16.4/23.5 | 14.0/17.6 |
No. atoms | |||
Protein | 2008 | 2007 | 863 |
Ligand | − | − | 13f |
Ion () | 15 | 30 | − |
Water | 431 | 41 | 143 |
B‐factors (Å2) | |||
Protein | 27.0 | 33.7 | 18.2 |
Ligand | − | − | 30.3 |
Ion () | 40.6 | 56.7 | − |
Water | 47.4 | 29.9 | 39.5 |
Model statistics | |||
rmsd bond length (Å) | 0.010 | 0.014 | 0.010 |
rmsd bond angles (°) | 1.33 | 1.67 | 1.64 |
Ramachandran plot (%) favoured/allowed/disallowed | 98.8/1.2/0 | 97.2/2.8/0 | 99.1/0.9/0 |
P65‐related MCU NTD/MCU NTD interactions are conserved in these three P65 crystal forms.
Beamline 5C and 7A at Pohang Accelerator Laboratory (PAL) in South Korea.
Values in parentheses are for highest‐resolution shell.
R merge = ∑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 over all reflections and ∑i is the sum over i measurements of reflection h.
R work = ∑hkl ¦¦Fo¦‐¦Fc¦¦/∑hkl¦Fo¦; 5% of the reflections were excluded for the R free calculation.
An unidentified electron density was observed and modeled with a tetraethylene glycol molecule.