6IGR
Crystal structure of S9 peptidase (S514A mutant in inactive state) from Deinococcus radiodurans R1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | RRCAT INDUS-2 BEAMLINE PX-BL21 |
| Synchrotron site | RRCAT INDUS-2 |
| Beamline | PX-BL21 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2018-09-08 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 0.97947 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 77.415, 189.200, 121.030 |
| Unit cell angles | 90.00, 108.59, 90.00 |
Refinement procedure
| Resolution | 39.756 - 2.600 |
| R-factor | 0.2181 |
| Rwork | 0.216 |
| R-free | 0.25270 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5yzm |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.711 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.300 | 2.640 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.096 | 0.710 |
| Rmeas | 0.113 | 0.845 |
| Rpim | 0.059 | 0.454 |
| Number of reflections | 100840 | 4992 |
| <I/σ(I)> | 11.4 | 2.1 |
| Completeness [%] | 99.7 | 99.9 |
| Redundancy | 3.5 | 3.3 |
| CC(1/2) | 0.995 | 0.743 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 5.28 | 294 | 40mM potassium phosphate, 16% PEG 8000, 20% glycerol |
