4XWK
P-glycoprotein co-crystallized with BDE-100
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-10-10 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.91929 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 89.000, 138.160, 185.150 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 92.570 - 3.500 |
R-factor | 0.2636 |
Rwork | 0.263 |
R-free | 0.28240 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4q9h |
RMSD bond length | 0.006 |
RMSD bond angle | 0.988 |
Data reduction software | MOSFLM (7.1.0) |
Data scaling software | Aimless (0.3.5) |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 92.570 | 92.570 | 3.710 |
High resolution limit [Å] | 3.500 | 10.500 | 3.500 |
Rmerge | 0.084 | 0.046 | 0.828 |
Rpim | 0.040 | 0.023 | 0.380 |
Total number of observations | 156577 | 5590 | 25243 |
Number of reflections | 29261 | ||
<I/σ(I)> | 10.2 | 25.2 | 2.2 |
Completeness [%] | 99.3 | 94.6 | 99.9 |
Redundancy | 5.4 | 4.9 | 5.4 |
CC(1/2) | 0.998 | 0.997 | 0.754 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.6 | 277 | PEG 600, Li2O4S, HEPES, EDTA |