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 |
