5IBY
Crystal structure of Enterococcus faecalis lipoate-protein ligase A (lplA-2) in complex with lipoic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-02-20 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.979054 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.977, 68.561, 54.154 |
| Unit cell angles | 90.00, 116.13, 90.00 |
Refinement procedure
| Resolution | 21.500 - 1.850 |
| R-factor | 0.1664 |
| Rwork | 0.164 |
| R-free | 0.21030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vqz |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.113 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP (11.1.03) |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.880 |
| High resolution limit [Å] | 1.850 | 5.020 | 1.850 |
| Rmerge | 0.036 | 0.032 | 0.161 |
| Rmeas | 0.040 | 0.036 | 0.186 |
| Rpim | 0.018 | 0.016 | 0.091 |
| Total number of observations | 139224 | ||
| Number of reflections | 28555 | ||
| <I/σ(I)> | 19.8 | ||
| Completeness [%] | 99.5 | 95.1 | 99.2 |
| Redundancy | 4.9 | 4.6 | 4 |
| CC(1/2) | 0.998 | 0.972 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.25 | 289 | 1.5 UL PROTEIN + 1.5 UL BUFFER (25% PEG3350, 0.1 M SODIUM CACODYLATE, 0.2 M SODIUM CHLORIDE, PH 5.25) |
