6FS7
Influenza A/California/04/2009 (pH1N1) endonuclease with I38T mutation with bound inhibitor, baloxavir acid (BXA)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-1 |
Synchrotron site | ESRF |
Beamline | MASSIF-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-10-18 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 0.966 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 135.680, 75.560, 121.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 90.637 - 1.960 |
R-factor | 0.189 |
Rwork | 0.188 |
R-free | 0.21140 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB:4AWK |
RMSD bond length | 0.004 |
RMSD bond angle | 0.799 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 90.637 | 2.010 |
High resolution limit [Å] | 1.960 | 1.960 |
Rmerge | 0.596 | |
Number of reflections | 94254 | 6540 |
<I/σ(I)> | 17.4 | 2.2 |
Completeness [%] | 99.4 | 99.7 |
Redundancy | 4.1 | 4 |
CC(1/2) | 0.994 | 0.767 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | Protein, at 15-17 mg/ml, was incubated with 10-fold molar excess of BXA for 30 min at RT, mixtures were centrifuged at RT for 5 minutes at 12000 g, and soluble fraction was used for crystallization trials (final protein concentration 8-10 mg/ml). Mother liquor was 0.2 M (NH4)2SO4, 0.1 M Na(CH3)2AsO2 pH 6.5, 30% (w/v) PEG8000 |