3SZ3
Crystal structure of Tryptophanyl-tRNA synthetase from Vibrio cholerae with an endogenous tryptophan
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-11 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.97903 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 76.020, 94.047, 47.036 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.090 - 1.500 |
| R-factor | 0.1606 |
| Rwork | 0.160 |
| R-free | 0.17900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n9i |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.458 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 1.530 |
| High resolution limit [Å] | 1.500 | 4.070 | 1.500 |
| Rmerge | 0.041 | 0.031 | 0.403 |
| Number of reflections | 54037 | ||
| <I/σ(I)> | 19.2 | ||
| Completeness [%] | 99.6 | 98.5 | 98.5 |
| Redundancy | 6.7 | 6.7 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7 | 60% Tascimate, pH 7, vapor diffusion |
