Table 1 Data collection and refinement statistics
From: Inward- and outward-facing X-ray crystal structures of homodimeric P-glycoprotein CmABCB1
QTA outward | Hg derivative (QTA outward) | QTA inward | |
|---|---|---|---|
Data collection | |||
Space group | P4132 | P4132 | R32 |
Cell dimensions | |||
a, b, c (Å) | 174.3, 174.3, 174.3 | 176.0, 176.0, 176.0 | 179.7, 179.7, 157.7 |
α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 120 |
Wavelength | 1.0000 | 1.00789 | 1.0000 |
Resolution (Å) | 43.6−1.89 (2.00−1.89)a | 50−2.70 (2.75−2.70)a | 47.1−3.02 (3.20−3.02)a |
R sym | 0.152 (1.187) | 0.148 (0.382) | 0.102 (0.629) |
Total reflections | 1,517,693 | 1,074,412 | 192,073 |
Unique reflections | 72,007 | 49,994 | 19,238 |
I /σI | 13.0 (1.9) | 51.6 (13.1) | 14.3 (2.4) |
Completeness (%) | 99.2 (95.4) | 100.0 (100.0) | 99.6 (98.5) |
Redundancy | 21.1 (18.2) | 21.5 (19.7) | 9.98 (10.1) |
CC1/2 (%) | 99.8 (74.0) | (98.3)b | 99.9 (91.8) |
Processing programs | XDS (ver. Jan. 26, 2018) | HKL2000 (ver. 0.98) | XDS (ver. Nov. 3, 2014) |
Refinement | |||
Resolution (Å) | 43.6−1.90 (1.95−1.90) | 47.1−3.02 (3.10−3.02) | |
No. reflections | 67,507 | 18,276 | |
Rwork/Rfree | 0.165/0.208 (0.289/0.293) | 0.226/0.275 (0.447/0.420) | |
No. atoms | |||
Protein | 4537 | 4476 | |
AMP-PNP | 31 | 0 | |
Mg2+ | 1 | 0 | |
Detergent | 67 | 63 | |
Water | 435 | 13 | |
B-factors (Å2) | |||
Protein | 62.7 | 91.3 | |
AMP-PNP | 23.5 | ||
Mg2+ | 22.8 | ||
Detergent | 68.6 | 120.2 | |
Water | 46.0 | 76.4 | |
R.m.s. deviations | |||
Bond lengths (Å) | 0.011 | 0.010 | |
Bond angles (°) | 1.537 | 1.490 | |
