7EV4
Crystal structure of the Lon-like protease MtaLonC with S582A mutation in complex with F-b20-Q
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 | 115.597, 115.597, 135.482 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.930 - 2.120 |
| R-factor | 0.1825 |
| Rwork | 0.180 |
| R-free | 0.22000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4fw9 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.799 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.200 |
| High resolution limit [Å] | 2.120 | 2.120 |
| Rmerge | 0.113 | 0.698 |
| Number of reflections | 58112 | 5772 |
| <I/σ(I)> | 21.5 | 3.9 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 11.5 | 11.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 295 | 10% isopropanol, 100 mM monosodium phosphate, 100 mM sodium citrate at pH 4.6. |
