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. |