Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-11-14 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9537 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 60.720, 73.261, 68.817 |
Unit cell angles | 90.00, 109.17, 90.00 |
Refinement procedure
Resolution | 45.160 - 1.840 |
Rwork | 0.188 |
R-free | 0.23210 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7mxz |
RMSD bond length | 0.010 |
RMSD bond angle | 1.575 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.160 | 1.880 |
High resolution limit [Å] | 1.840 | 1.840 |
Rmerge | 0.100 | 1.367 |
Rpim | 0.042 | 0.587 |
Number of reflections | 24629 | 1295 |
<I/σ(I)> | 9.4 | 1.3 |
Completeness [%] | 99.0 | 85.7 |
Redundancy | 6.7 | |
CC(1/2) | 0.998 | 0.574 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | Protein was at 10 mg/mL and the drops were 200 nL plus 200 nL with the reservoir being 22.5% PEG 3350, 0.3M MgCl2, 0.1M Na-HEPES pH 6.55 |