8KHS
the structure of a glutamine amidotransferase DnfC from Alcaligenes sp.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-11-04 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9785 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 66.176, 78.403, 86.324 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.201 - 2.100 |
R-factor | 0.2454 |
Rwork | 0.244 |
R-free | 0.28130 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.634 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.14_3260: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.210 | 2.160 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.069 | 1.081 |
Rmeas | 0.072 | 1.147 |
Rpim | 0.021 | 0.374 |
Number of reflections | 13421 | 1069 |
<I/σ(I)> | 18.5 | |
Completeness [%] | 99.8 | 98.6 |
Redundancy | 12 | |
CC(1/2) | 0.999 | 0.913 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 4% Tacsimate pH 5.0, 10% PEG 3350 |