7S3V
Structure of HsKYNase_66, an evolved variant of human kynureninase with greatly increased activity towards kynurenine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 93 |
Detector technology | PIXEL |
Collection date | 2017-11-15 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.03322 |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 140.890, 140.890, 286.371 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.344 - 3.249 |
R-factor | 0.1896 |
Rwork | 0.185 |
R-free | 0.22780 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2hzp |
RMSD bond length | 0.004 |
RMSD bond angle | 0.732 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 3.310 |
High resolution limit [Å] | 3.249 | 8.810 | 3.250 |
Rmerge | 0.164 | 0.056 | 0.791 |
Rmeas | 0.191 | 0.065 | 0.921 |
Rpim | 0.095 | 0.032 | 0.460 |
Number of reflections | 21474 | 1079 | 1064 |
<I/σ(I)> | 4.3 | ||
Completeness [%] | 92.7 | 84.2 | 94.7 |
Redundancy | 3.6 | 3.5 | 3.6 |
CC(1/2) | 0.992 | 0.574 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277 | 8% PEG8000, 100 mM imidazole, 50 mM MgCl2, 0.2 mM PLP, 5% sucrose (diffracting crystal proteins were briefly supplemented with 0.005 mg/mL trypsin prior to sitting drop vapor diffusion in order to remove flexible terminal ends). |