7EUX
Crystal structure of the Lon-like protease MtaLonC with D581A 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 | 115.742, 115.742, 135.998 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.830 - 2.250 |
| R-factor | 0.155 |
| Rwork | 0.153 |
| R-free | 0.19300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4fw9 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.454 |
| 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] | 20.000 | 2.330 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.063 | 0.592 |
| Number of reflections | 48531 | 4799 |
| <I/σ(I)> | 23.7 | 2.1 |
| Completeness [%] | 99.2 | 98.2 |
| Redundancy | 5.2 | 4.7 |
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. |
