6MVU
Structure of a bacterial ALDH16 active site mutant C295A complexed with p-nitrophenylacetate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-11-02 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.9791 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 79.383, 119.623, 158.670 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 95.519 - 1.488 |
R-factor | 0.1928 |
Rwork | 0.192 |
R-free | 0.21580 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | homology model built with Swiss-Model using 5kf6 as the template |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.23) |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 119.620 | 1.510 |
High resolution limit [Å] | 1.488 | 1.488 |
Rmerge | 0.133 | 1.799 |
Rmeas | 0.144 | 1.952 |
Rpim | 0.055 | 0.748 |
Number of reflections | 470410 | 11001 |
<I/σ(I)> | 8.8 | |
Completeness [%] | 98.8 | 90.8 |
Redundancy | 6.7 | 6.5 |
CC(1/2) | 0.998 | 0.440 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | Protein was concentrated to 6 mg/ml in a storage buffer consisting of 20 mM Tris-HCl at pH 8.0, 100 mM NaCl, 2.5% glycerol and 0.5 mM TCEP. The crystallization reservoir solution contained 20% (w/v) polyethylene glycol (PEG) 3350, 200 mM ammonium sulfate and 100 mM Bis-Tris at pH 5.5. |