7EUY
Crystal structure of the Lon-like protease MtaLonC with D582A mutation in complex with substrate polypeptide
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 | 2011-06-10 |
| Detector | BRUKER SMART 6500 |
| Wavelength(s) | 1 |
| Spacegroup name | P 6 |
| Unit cell lengths | 115.838, 115.838, 135.455 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.460 - 2.200 |
| R-factor | 0.1839 |
| Rwork | 0.182 |
| R-free | 0.21130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4fw9 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.658 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.086 | 0.655 |
| Number of reflections | 52084 | 5127 |
| <I/σ(I)> | 26.6 | 3.3 |
| Completeness [%] | 99.7 | 98.7 |
| Redundancy | 7.6 | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 295 | 10% isopropanol, 100 mM monosodium phosphate and 100 mM sodium citrate at pH 4.6 |
