2C8M
Structure of protein Ta0514, putative lipoate protein ligase from T. acidophilum with bound lipoic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.377, 117.882, 105.663 |
| Unit cell angles | 90.00, 93.51, 90.00 |
Refinement procedure
| Resolution | 53.300 - 1.890 |
| R-factor | 0.208 |
| Rwork | 0.207 |
| R-free | 0.23900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2c7i |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.095 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.300 | 2.080 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.064 | 0.210 |
| Number of reflections | 97539 | |
| <I/σ(I)> | 20 | 5.4 |
| Completeness [%] | 99.2 | 99.2 |
| Redundancy | 4 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.7 | 293 | pH 6.70 |
