4KSD
Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-11-10 |
Detector | MARMOSAIC 325 mm CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 87.100, 102.470, 312.100 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 61.071 - 4.100 |
R-factor | 0.3239 |
Rwork | 0.323 |
R-free | 0.34450 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 1.072 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 61.071 |
High resolution limit [Å] | 4.100 |
Number of reflections | 22783 |
Completeness [%] | 95.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 277 | 0.1 M Hepes (pH 7-8) and 22-27% (w/v) PEG 600, VAPOR DIFFUSION, SITTING DROP, temperature 277K |