4LSG
Structure of Mouse P-Glycoprotein
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-12-16 |
Detector | MARMOSAIC 300 |
Wavelength(s) | 1.00695, 1.00923 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 97.542, 115.426, 378.858 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.983 - 3.800 |
R-factor | 0.3378 |
Rwork | 0.336 |
R-free | 0.35690 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ksb |
RMSD bond length | 0.006 |
RMSD bond angle | 1.309 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX (1.8.2_1309) |
Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 4.040 |
High resolution limit [Å] | 3.800 | 3.800 |
Number of reflections | 41131 | |
Completeness [%] | 96.1 | 86.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 278 | 17% PEG 350mme, 0.05M tris, 0.04% sodium cholate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 278K |