5ZBI
Crystal structure of asparaginyl endopeptidases from Viola Canadensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-11-02 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9537 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 184.470, 62.080, 82.910 |
| Unit cell angles | 90.00, 106.81, 90.00 |
Refinement procedure
| Resolution | 44.420 - 2.090 |
| R-factor | 0.191 |
| Rwork | 0.189 |
| R-free | 0.22500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5h0i |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.050 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.10.3) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 88.300 | 2.210 |
| High resolution limit [Å] | 2.090 | 2.090 |
| Rmerge | 0.099 | 0.671 |
| Rpim | 0.055 | 0.372 |
| Number of reflections | 53019 | 30795 |
| <I/σ(I)> | 12 | 2.3 |
| Completeness [%] | 99.7 | 98.1 |
| Redundancy | 4.2 | 4.1 |
| CC(1/2) | 0.997 | 0.719 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | Ammonium Sulfate, Bis-Tris pH 5.5, PEG 3350. |
