5FRK
SeMet crystal structure of Erwinia amylovora AmyR amylovoran repressor, a member of the YbjN protein family
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I03 |
Synchrotron site | Diamond |
Beamline | I03 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 138.028, 49.618, 57.813 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 69.010 - 2.120 |
R-factor | 0.21887 |
Rwork | 0.216 |
R-free | 0.27584 |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.015 |
RMSD bond angle | 1.778 |
Data reduction software | XDS |
Data scaling software | SCALEPACK |
Phasing software | SHELX |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 53.340 | 2.180 |
High resolution limit [Å] | 2.120 | 2.120 |
Rmerge | 0.090 | 1.000 |
Number of reflections | 22681 | |
<I/σ(I)> | 24 | 1.4 |
Completeness [%] | 97.2 | 75.4 |
Redundancy | 12.9 | 8.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.3 | 293 | 0.1 M SODIUM CACODYLATE PH7.3 0.3 M MAGNESIUM CHLORIDE, 42% PEG 200, 293 K PROTEIN CONCENTRATION 8 MG/ML |