3SP1
Crystal structure of cysteinyl-tRNA synthetase (cysS) from Borrelia burgdorferi
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-05-28 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97740 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 62.620, 49.890, 179.630 |
| Unit cell angles | 90.00, 93.18, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.550 |
| R-factor | 0.2268 |
| Rwork | 0.224 |
| R-free | 0.27398 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1li5 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.538 |
| Data scaling software | XSCALE |
| Phasing software | PHASER (2.1.4) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.620 | |
| High resolution limit [Å] | 2.550 | 11.400 | 2.550 |
| Rmerge | 0.107 | 0.034 | 0.524 |
| Number of reflections | 36598 | ||
| <I/σ(I)> | 12.48 | 37.12 | 2.52 |
| Completeness [%] | 99.5 | 78.7 | 99 |
| Redundancy | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | protein at 25 mg/mL against PACT E9 25% PEG 3350, 0.2 M Na K Tartrate with 25% ethylene glycol as cryo-protectant, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
