4A01
Crystal Structure of the H-Translocating Pyrophosphatase
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 218.619, 88.241, 159.105 |
| Unit cell angles | 90.00, 125.53, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.350 |
| R-factor | 0.16981 |
| Rwork | 0.168 |
| R-free | 0.20314 |
| Structure solution method | MAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.056 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.430 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.080 | 0.500 |
| Number of reflections | 100220 | |
| <I/σ(I)> | 20.8 | 2.7 |
| Completeness [%] | 98.7 | 98.5 |
| Redundancy | 3.84 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
