6IGP
Crystal structure of S9 peptidase (inactive state)from Deinococcus radiodurans R1 in P212121
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 | CCD |
| Collection date | 2015-09-29 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97947 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 119.857, 130.492, 194.973 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.740 - 2.400 |
| R-factor | 0.1866 |
| Rwork | 0.185 |
| R-free | 0.21690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5yzm |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.877 |
| 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] | 48.740 | 2.440 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.156 | 0.865 |
| Rmeas | 0.165 | 0.912 |
| Rpim | 0.052 | 0.288 |
| Number of reflections | 119902 | 5851 |
| <I/σ(I)> | 14.9 | 3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10 | 10 |
| CC(1/2) | 0.998 | 0.876 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 5.31 | 294 | 50mM Tris-Cl pH 8.5, 200mM ammonium-citrate, 10mM calcium chloride, 14 % PEG 3350 |
