4C3Z
Nucleotide-free crystal structure of nucleotide-binding domain 1 from human MRP1 supports a general-base catalysis mechanism for ATP hydrolysis.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-02-21 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 31 |
| Unit cell lengths | 64.299, 64.299, 65.491 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 42.423 - 2.100 |
| R-factor | 0.1651 |
| Rwork | 0.164 |
| R-free | 0.19410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2cbz |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.178 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.420 | 2.160 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.070 | 0.610 |
| Number of reflections | 17692 | |
| <I/σ(I)> | 7.7 | 1.9 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 25% PEG 3.350, 0.2M AMSO4, 0.1M BISTRIS PH5.5 |
