5B6L
Structure of Deg protease HhoA from Synechocystis sp. PCC 6803
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-06-08 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9793 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 135.359, 135.359, 114.386 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.389 - 2.801 |
| R-factor | 0.2399 |
| Rwork | 0.239 |
| R-free | 0.26680 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3qo6 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.320 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.060 | 0.622 |
| Number of reflections | 10074 | |
| <I/σ(I)> | 38 | 4 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 10.7 | 11.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.3 | 277 | 20% PEG 4000, 100 mM Sodium acetate |
