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 | 2018-11-30 |
Detector | DECTRIS EIGER X 4M |
Wavelength(s) | 0.9677 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.280, 57.944, 66.947 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.812 - 1.432 |
Rwork | 0.185 |
R-free | 0.20580 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ati |
RMSD bond length | 0.013 |
RMSD bond angle | 1.784 |
Data reduction software | XDS (VERSION Jan 26, 2018 BUILT=20180126) |
Data scaling software | Aimless (0.7.3) |
Phasing software | PHASER (2.8.2) |
Refinement software | REFMAC (5.8.0238 2018/15/10) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.480 |
High resolution limit [Å] | 1.430 | 1.430 |
Rmeas | 0.100 | 1.719 |
Rpim | 0.043 | 0.751 |
Number of reflections | 39193 | 3704 |
<I/σ(I)> | 11.6 | 0.9 |
Completeness [%] | 99.1 | 97.2 |
Redundancy | 5.3 | 4.9 |
CC(1/2) | 0.998 | 0.430 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 15 mg/ml protein, 100 mM benzamidine, 25% PEG 8000, 0.2 M ammonium sulfate, 100 mM Tris-HCl |