7N8W
Crystal structure of ERI2 nuclease bound to rAMP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 12.3.1 |
Synchrotron site | ALS |
Beamline | 12.3.1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-09-22 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.11583 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 60.832, 56.338, 75.852 |
Unit cell angles | 90.00, 104.57, 90.00 |
Refinement procedure
Resolution | 44.690 - 2.350 |
R-factor | 0.1812 |
Rwork | 0.179 |
R-free | 0.22270 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4l83 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.539 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.390 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmeas | 0.104 | 0.550 |
Number of reflections | 19057 | 1820 |
<I/σ(I)> | 27.9 | |
Completeness [%] | 90.8 | |
Redundancy | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 288 | 9% MPEG 2K, 1% saturated Magnesium Sulfate, 5% Ethylene glycol, 200 mM Imidazole Malate buffer pH 5.4 |