5ICL
Crystal structure of Enterococcus faecalis lipoate-protein ligase A (lplA-2) in complex with lipoyl-AMP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-12-06 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0332 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.942, 69.350, 97.685 |
| Unit cell angles | 90.00, 92.15, 90.00 |
Refinement procedure
| Resolution | 48.000 - 1.800 |
| R-factor | 0.1994 |
| Rwork | 0.198 |
| R-free | 0.23510 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5iby |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.165 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 48.800 | 1.830 |
| High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
| Rmerge | 0.058 | 0.025 | 0.354 |
| Number of reflections | 62746 | ||
| <I/σ(I)> | 11.5 | ||
| Completeness [%] | 99.7 | 99.1 | 99.7 |
| Redundancy | 4.2 | 4.1 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.25 | 289 | 1.5 UL PROTEIN + 1.5 UL BUFFER (31% PEG3350, 0.1 M SODIUM CACODYLATE, 0.2 M SODIUM CHLORIDE, PH 5.25) |
