2V7F
Structure of P. abyssi RPS19 protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 32.700, 57.430, 80.200 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.570 - 1.150 |
| R-factor | 0.138 |
| Rwork | 0.137 |
| R-free | 0.15500 |
| Structure solution method | MIRAS |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.818 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | SHARP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.000 | 1.250 |
| High resolution limit [Å] | 1.150 | 1.150 |
| Rmerge | 0.060 | 0.210 |
| Number of reflections | 49876 | |
| <I/σ(I)> | 22.25 | 6.12 |
| Completeness [%] | 91.5 | 72.3 |
| Redundancy | 7.5 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 30% - 36% PEG 2000MME TRIS-HCL 100MM PH 6.8 - 7.5 |
