1X2H
Crystal Structure of Lipate-Protein Ligase A from Escherichia coli complexed with lipoic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-02-07 |
| Detector | Bruker DIP-6040 |
| Wavelength(s) | 0.92154 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 83.200, 111.600, 289.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 66.670 - 2.910 |
| R-factor | 0.1907 |
| Rwork | 0.186 |
| R-free | 0.27140 |
| Structure solution method | Difference Fourier |
| Starting model (for MR) | Lipoate protein ligase A from E. coli |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.976 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 200.000 | 3.000 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.120 | 0.421 |
| Number of reflections | 29247 | |
| <I/σ(I)> | 15.6 | 3.8 |
| Completeness [%] | 97.4 | 99 |
| Redundancy | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | ethylene glycol, glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
