6N67
Crystal structure of the ligase domain of fungal tRNA ligase Trl1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-06-22 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 1.033 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.729, 56.580, 173.879 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.740 - 1.900 |
| R-factor | 0.1717 |
| Rwork | 0.170 |
| R-free | 0.21440 |
| Structure solution method | SAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.386 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.5.27) |
| Phasing software | CRANK2 |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 37.740 | 37.740 | 1.940 |
| High resolution limit [Å] | 1.900 | 9.110 | 1.900 |
| Rmerge | 0.063 | 0.027 | 1.029 |
| Rmeas | 0.073 | 0.032 | 1.184 |
| Rpim | 0.036 | 0.015 | 0.575 |
| Total number of observations | 159936 | ||
| Number of reflections | 39302 | 436 | 2495 |
| <I/σ(I)> | 10.3 | ||
| Completeness [%] | 99.3 | 98.9 | 99.1 |
| Redundancy | 4.1 | 3.7 | 4.1 |
| CC(1/2) | 0.998 | 0.998 | 0.793 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 293 | ammonium sulfate, sodium chloride, HEPES |
