Table 1.
Data reduction and refinement statistics.
| Processing | MhsT‐Tyr | MhsT‐4FPhe | MhsT‐Phe | MhsT‐Ile c | MhsT‐Leu b | MhsT‐Val b |
|---|---|---|---|---|---|---|
| Beamline | DLS‐I24 | DLS‐I04 | DLS‐I24 | SLS‐ PXI | DLS‐I04 | DLS‐I24 |
| Space group | P2 | P2 | P2 | P21 | P21 | P21 |
| Unit cell dimensions | ||||||
| a, b, c (Å) | 44.1, 49.9, 110.3 | 44.2, 49.9, 109.7 | 44.4, 49.9, 110.1 | 44.0, 97.3, 110.9 | 44.2, 215.6, 50.2 | 44.1, 216.1, 50.4 |
| α, β, γ (°) | 90.0, 96.8, 90.0 | 90.0, 96.1, 90.0 | 90.0, 96.8, 90.0 | 90.0, 96.1, 90.0 | 90.0, 90.05, 90.0 | 90.0, 90.02, 90.0 |
| Wavelength (Å) | 0.96864 | 0.96858 | 0.96860 | 1.00001 | 0.97949 | 0.97950 |
| No. reflections a | 69,099 (6,707) | 40,499 (4,060) | 41,999 (4,369) | 37,578 (6,463) | 114,897 (5,823) | 97,704 (9,611) |
| Resolution a | 29.8–2.30 (2.38–2.30) | 43.9–2.26 (2.33–2.26) | 45.5–2.25 (2.32–2.25) | 43.7–3.10 (3.31–3.10) | 45.5–2.35 (2.43–2.35) | 29.1–2.60 (2.72–2.60) |
| R merge a | 0.119 (0.734) | 0.118 (0.677) | 0.120 (0.820) | 0.195 (0.815) | 0.096 (0.679) | 0.117 (0.950) |
| R pim a | 0.077 (0.595) | 0.091 (0.532) | 0.083 (0.563) | 0.124 (0.532) | 0.066 (0.502) | 0.075 (0.607) |
| I/σI a | 7.8 (1.6) | 5.3 (1.3) | 7.3 (2.1) | 3.6 (1.2) | 8.1 (1.4) | 8.0 (1.2) |
| Completeness (%) a | 97.4 (95.2) | 92.9 (93.9) | 98.2 (99.3) | 81.6 (83.8) | 98.5 (98.5) | 99.5 (99.7) |
| Redundancy a | 3.3 (3.34) | 2.3 (1.3) | 2.9 (3.0) | 2.7 (2.5) | 3.0 (2.6) | 3.4 (3.4) |
| CC1/2 a | 0.991 (0.472) | 0.991 (0.472) | 0.989 (0.488) | 0.989 (0.636) | 0.996 (0.511) | 0.994 (0.489) |
| Wilson B‐factor | 39.2 | 34.3 | 38.2 | 63.0 | 37.4 | 49.3 |
| Twin fraction | N/A | N/A | N/A | N/A | 0.443 | (0.065) |
| Refinement | ||||||
| Resolution (Å) a | 29.8–2.30 (2.38–2.30) | 39.3–2.26 (2.34–2.26) | 45.4–2.25 (2.33–2.25) | 43.7–3.10 (3.31–3.10) | 45.5–2.35 (2.43–2.35) | 49.1–2.60 (2.69–2.60) |
| R work/R free | 0.223/0.263 (0.254/0.305) | 0.223/0.261 (0.291/0.299) | 0.224/0.255 (0.305/0.356) | 0.277/0.305 (0.340/0.355) | 0.185/0.222 (0.260/0.304) | 0.207/0.237 (0.306/0.355) |
| No. atoms | ||||||
| Protein | 3,324 | 3,324 | 3,315 | 6,630 | 6,678 | 6,674 |
| Ligand | 13 | 13 | 12 | 18 | 18 | 16 |
| Sodium | 2 | 2 | 2 | 4 | 4 | 4 |
| Detergent | 103 | 195 | 107 | 109 | 176 | 357 |
| Water | 63 | 28 | 59 | 17 | 46 | 73 |
| B‐ factors (Å2) | ||||||
| Protein | 36.2 | 38.2 | 45.0 | 56.7 | 41.4 | 56.9 |
| Ligand | 26.1 | 28.7 | 31.8 | 52.6 | 34.1 | 48.8 |
| Sodium | 28.8 | 26.7 | 34.4 | 52.8 | 33.3 | 49.6 |
| Detergent | 47.9 | 55.8 | 64.1 | 58.2 | 51.7 | 68,4 |
| Water | 38.5 | 43.3 | 47.9 | 52.2 | 37.9 | 55.4 |
| R.m.d. deviations | ||||||
| Bond length (Å) | 0.002 | 0.003 | 0.002 | 0.002 | 0.002 | 0.003 |
| Bond angles (o) | 0.542 | 0.601 | 0.583 | 0.578 | 0.505 | 0.595 |
| Ramachandran | ||||||
| Favoured (%) | 97.7 | 98.82 | 98.2 | 95.7 | 96.9 | 96.4 |
| Outliers (%) | 0 | 0 | 0 | 0.23 | 0 | 0 |
a
Values in parentheses are for highest resolution shell.
b
MhsT‐Leu was refined against the h,‐k,‐l twin law with 44.3% twinning, whereas MhsT‐Val was refined without use of twin law.
c
The refinement of the MhsT‐Ile complex was hindered by low completeness and the presence of translational NCS. Initial difference maps were consistent with the binding mode observed for the other aliphatic substrates.