4I4C
Crystal structure of the protein frsA complexed with unknown ligand
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-01-25 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.075 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.659, 104.542, 82.302 |
| Unit cell angles | 90.00, 91.18, 90.00 |
Refinement procedure
| Resolution | 38.284 - 1.950 |
| R-factor | 0.1819 |
| Rwork | 0.179 |
| R-free | 0.22730 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3mve |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.053 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | BALBES |
| Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 38.284 |
| High resolution limit [Å] | 1.950 |
| Number of reflections | 51363 |
| Completeness [%] | 97.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 20% PEG monomethyl ether 2000, 0.1M Tris, 0.2M Trimethylamine N-oxide, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K |
