5ICH
Crystal structure of Enterococcus faecalis lipoate-protein ligase A (lplA-2) in complex with 8BO-AMP
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) | 0.97905 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.917, 69.383, 97.664 |
| Unit cell angles | 90.00, 92.30, 90.00 |
Refinement procedure
| Resolution | 21.500 - 1.850 |
| R-factor | 0.1712 |
| Rwork | 0.169 |
| R-free | 0.20520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5iby |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.186 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP (11.0.05) |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 3.990 | 1.850 |
| Rmerge | 0.037 | 0.026 | 0.126 |
| Rmeas | 0.041 | 0.030 | 0.145 |
| Rpim | 0.018 | 0.013 | 0.070 |
| Total number of observations | 282553 | ||
| Number of reflections | 58160 | ||
| <I/σ(I)> | 23.7 | ||
| Completeness [%] | 99.8 | 98.2 | 100 |
| Redundancy | 4.9 | 4.7 | 4.1 |
| CC(1/2) | 0.999 | 0.984 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.25 | 289 | 1.5 UL PROTEIN + 1.5 UL BUFFER (27% PEG3350, 0.1 M SODIUM CACODYLATE, 0.2 M SODIUM CHLORIDE, PH 5.25) |
