4HK4
Crystal structure of apo Tyrosine-tRNA ligase mutant protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2010-06-29 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 2 1 |
| Unit cell lengths | 52.695, 38.886, 83.061 |
| Unit cell angles | 90.00, 90.98, 90.00 |
Refinement procedure
| Resolution | 31.287 - 2.298 |
| R-factor | 0.2314 |
| Rwork | 0.229 |
| R-free | 0.27660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1j1u |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.662 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.6.2_432)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.380 |
| High resolution limit [Å] | 2.290 | 2.300 |
| Rmerge | 0.053 | 0.265 |
| Number of reflections | 14520 | |
| <I/σ(I)> | 30.4 | 4.97 |
| Completeness [%] | 94.8 | 70.5 |
| Redundancy | 5 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.1 | 289 | protein sample (40mg/ml) in 25mM Tris-Cl PH8.0, 50mM NaCl mixed with equal volume of reservior solution containing 20-22% PEG3350, 0.2M (NH4)2SO4, 0.1M sodium citrate PH6.1-6.2, for 5 days, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
