4N9H
Crystal structure of Transcription regulation Protein CRP
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE AR-NW12A |
Synchrotron site | Photon Factory |
Beamline | AR-NW12A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-10-18 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 0.97922 |
Spacegroup name | P 61 |
Unit cell lengths | 120.617, 120.617, 60.349 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.200 |
R-factor | 0.20494 |
Rwork | 0.202 |
R-free | 0.26331 |
Structure solution method | MAD |
RMSD bond length | 0.019 |
RMSD bond angle | 2.432 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.010 | 2.240 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.086 | 0.394 |
Number of reflections | 25544 | |
<I/σ(I)> | 12.3 | |
Completeness [%] | 99.7 | 100 |
Redundancy | 22.5 | 21.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.4 | 293 | PEG 8000, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |