9D65
Nitrile hydratase BR52A mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2022-10-10 |
Detector | MAR CCD 300 mm |
Wavelength(s) | 0.97856 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 65.964, 65.964, 186.400 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 31.220 - 1.450 |
R-factor | 0.2419 |
Rwork | 0.240 |
R-free | 0.27890 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 0.820 |
Data reduction software | Adxv |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((1.21rc1_5156: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.220 | 3.925 |
High resolution limit [Å] | 1.450 | 1.450 |
Rmerge | 0.168 | 0.967 |
Number of reflections | 84526 | 8359 |
<I/σ(I)> | 8.8 | 2.1 |
Completeness [%] | 99.4 | 100 |
Redundancy | 10.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 1.2 M sodium citrate tribasic in 0.1 M HEPES at pH 7.5 |