Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-3 |
Synchrotron site | ESRF |
Beamline | MASSIF-3 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-06-30 |
Detector | DECTRIS EIGER X 4M |
Wavelength(s) | 0.9677 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 75.512, 143.173, 335.372 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 132.024 - 3.325 |
Rwork | 0.204 |
R-free | 0.26750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4wsb |
RMSD bond length | 0.003 |
RMSD bond angle | 1.217 |
Data reduction software | XDS |
Data scaling software | autoPROC |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0257) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 132.024 | 3.463 |
High resolution limit [Å] | 3.325 | 3.325 |
Rmerge | 0.190 | 2.298 |
Rmeas | 0.199 | 2.388 |
Rpim | 0.057 | |
Number of reflections | 50439 | 2523 |
<I/σ(I)> | 10.7 | 1.5 |
Completeness [%] | 92.7 | 42.2 |
Redundancy | 11.6 | 13.3 |
CC(1/2) | 0.997 | 0.500 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 281 | Protein at about 9 mg/ml 0.1 M Tris pH 7.0, 8-13% PEG 8K, 0.2 M MgCl2, 0.1 M guanidine hydrochloride |