3A7A
Crystal structure of E. coli lipoate-protein ligase A in complex with octyl-amp and apoH-protein
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 | 2009-03-06 |
| Detector | Bruker DIP-6040 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 70.013, 102.016, 159.934 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.100 |
| R-factor | 0.23223 |
| Rwork | 0.228 |
| R-free | 0.27855 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2e5a |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.636 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.110 |
| High resolution limit [Å] | 2.960 | 3.000 |
| Rmerge | 0.070 | 0.484 |
| Number of reflections | 23803 | |
| <I/σ(I)> | 19.7 | 2 |
| Completeness [%] | 98.1 | 97 |
| Redundancy | 4.1 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 16.2% PEG 3350, 0.045M MgSO4, 0.045M NaCl, 1mM NiCl2, 2% Polyethylene glycol monomethyl ether 2000, 0.01M Tris-Cl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
