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 |