5UK3
Crystal structure of cyanase from T. urticae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-06-23 |
Detector | RAYONIX MX300-HS |
Wavelength(s) | 1.000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 71.074, 81.611, 136.466 |
Unit cell angles | 90.00, 100.37, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.800 |
R-factor | 0.22159 |
Rwork | 0.221 |
R-free | 0.23997 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2iv1 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.668 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.850 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.069 | 0.546 |
Rmeas | 0.102 | 0.721 |
Rpim | 0.050 | 0.350 |
Number of reflections | 38010 | 1906 |
<I/σ(I)> | 22.5 | 2 |
Completeness [%] | 99.9 | 100 |
Redundancy | 4.1 | 4.2 |
CC(1/2) | 0.800 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 298 | 0.1 M Tris pH 7.5, 15% PEG6000 |