5H45
Crystal structure of the C-terminal Lon protease-like domain of Thermus thermophilus RadA/Sms
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-02-08 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 43 3 2 |
| Unit cell lengths | 156.289, 156.289, 156.289 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.420 - 2.700 |
| R-factor | 0.19908 |
| Rwork | 0.196 |
| R-free | 0.24997 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.622 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.750 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Number of reflections | 18550 | |
| <I/σ(I)> | 20.4 | 1.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 41.3 | 41.6 |
| CC(1/2) | 0.625 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 7.5 | 277.15 | 4mg/mL protein, 50mM Tris-HCl, 500mM sodium chloride |
