9FTF
Crystal structure of the Connecting Domain of the Nipah virus Large protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-09-21 |
Detector | DECTRIS EIGER2 XE 16M |
Wavelength(s) | 0.95373 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 40.760, 50.540, 61.100 |
Unit cell angles | 90.00, 95.71, 90.00 |
Refinement procedure
Resolution | 60.800 - 1.850 |
R-factor | 0.1946 |
Rwork | 0.193 |
R-free | 0.21850 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.002 |
RMSD bond angle | 0.552 |
Data reduction software | DIALS |
Data scaling software | xia2 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.800 | 10.000 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.102 | |
Number of reflections | 19413 | 19413 |
<I/σ(I)> | 10.3 | |
Completeness [%] | 91.3 | 91.55 |
Redundancy | 6 | |
CC(1/2) | 0.998 | 0.998 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 293.15 | 35% tert-Butanol 0.1M tri-Sodium Citrate pH 5.6 |