6LND
Crystal structure of transposition protein TniQ
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 | 2019-08-11 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.9794 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 66.277, 66.277, 178.584 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.001 |
R-factor | 0.1944 |
Rwork | 0.192 |
R-free | 0.22830 |
Structure solution method | SAD |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | AutoSol |
Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 4.310 | 2.000 |
Rmerge | 0.096 | 0.061 | 0.702 |
Rmeas | 0.100 | 0.063 | 0.727 |
Rpim | 0.027 | 0.017 | 0.190 |
Number of reflections | 51187 | 3048 | 2711 |
<I/σ(I)> | 6.5 | ||
Completeness [%] | 100.0 | 99.8 | 100 |
Redundancy | 14.2 | 13.4 | 14.4 |
CC(1/2) | 0.986 | 0.935 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 8.7 | 293 | 0.1 M Tris-HCl (pH 8.7), 2% Polyethylene glycol 8000 (w/v) |