1TC5
Structural Analysis of a probable eukaryotic D-amino acid tRNA deacylase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-11-14 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.91840 |
| Spacegroup name | P 2 2 21 |
| Unit cell lengths | 67.479, 67.465, 174.410 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.130 - 1.930 |
| R-factor | 0.20053 |
| Rwork | 0.199 |
| R-free | 0.23430 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | SeMAD model which crystallized in a different space group (p21) |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.279 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.673 | 2.020 |
| High resolution limit [Å] | 1.930 | 1.930 |
| Rmerge | 0.058 | 0.238 |
| Number of reflections | 48177 | |
| <I/σ(I)> | 10.2 | 2 |
| Completeness [%] | 79.4 | 28.6 |
| Redundancy | 3.1 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | PEG 200, MES, PEG3000, pH 6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |






