Table 2 X-ray data collection, phasing, and refinement statistics
From: Structure and inhibition mechanism of the catalytic domain of human squalene epoxidase
SQLE•FAD• Cmpd-4′′ | SeMet-SQLE•FAD•Cmpd-4′′ | SQLE•FAD• NB-598 | SQLE•FAD | |||
|---|---|---|---|---|---|---|
Native | Peak | Inflection | Remote | |||
PDB:6C6N | PDB:6C6P | PDB:6C6R | ||||
Data collection | ||||||
Wavelength (Å) | 0.97941 | 0.97909 | 0.97959 | 0.96108 | 0.97915 | 0.9792 |
Space group | P3221 | P3221 | P3221 | P3221 | P3221 | P3221 |
Cell dimensions | ||||||
a (Å) | 126.96 | 127.1 | 127.2 | 127.23 | 127.86 | 126.39 |
b (Å) | 126.36 | 127.1 | 127.2 | 127.23 | 127.86 | 126.39 |
c (Å) | 166.12 | 165.91 | 166.14 | 166.24 | 165.09 | 166.01 |
α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
Resolutiona (Å) | 35.79–2.30 | 50–2.75 | 50–2.90 | 50–3.15 | 40.57–2.50 | 38.81–3.00 |
(2.38–2.30) | (2.80-2.75) | (2.95–2.90) | (3.20–3.15) | (2.59–2.50) | (3.11–3.00) | |
Rmergea (%) | 8.2 (55.5) | 9.0 (53.5) | 8.0 (51.8) | 8.5 (48.9) | 8.6 (54.1) | 12.4 (68.8) |
I/σIa | 12.1 (3.0) | 52.1 (7.7) | 39.7 (5.1) | 37.7 (6.4) | 15.1 (2.5) | 10.6 (2.5) |
Completenessa (%) | 98.8 (99.7) | 100 (100) | 100 (100) | 99.9 (100) | 88.5 (89.3) | 99.6 (98.8) |
Redundancya | 5.2 (5.3) | 18.4 (18.8) | 9.1 (9.4) | 9.1 (9.3) | 4.8 (4.7) | 7.4 (6.1) |
Figure of merit (post-density modification) | 0.24/0.74 | |||||
Rcullis (anomalous) | 0.84 | |||||
Refinement | ||||||
No. reflections | 68379 | 48318 | 31143 | |||
Rwork/Rfree (%) | 18.90/22.00 | 19.31/23.42 | 19.01/24.85 | |||
No. of atoms | ||||||
Protein | 7058 | 7050 | 7060 | |||
Ligand | 401 | 363 | 315 | |||
Water | 179 | 170 | 58 | |||
B-factors (Å2) | ||||||
Protein | 53.46 | 59.69 | 61.32 | |||
Ligand | 57.33 | 61.35 | 57.17 | |||
Water | 47.31 | 55.42 | 44.68 | |||
R.m.s deviations | ||||||
Bond lengths (Å) | 0.003 | 0.009 | 0.004 | |||
Bond angles (°) | 0.58 | 0.99 | 0.68 | |||
