2CBZ
Structure of the human Multidrug Resistance Protein 1 Nucleotide Binding Domain 1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | P 31 |
Unit cell lengths | 65.560, 65.560, 64.612 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 1.500 |
R-factor | 0.161 |
Rwork | 0.160 |
R-free | 0.18700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1xmi |
RMSD bond length | 0.007 |
RMSD bond angle | 1.194 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.580 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.060 | 0.430 |
Number of reflections | 49722 | |
<I/σ(I)> | 14.1 | 2.9 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 14.1 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 8% PEG1000, 0.1M MG ACETATE PH 5.6 |