5Z97
Crystal structure of a lactonase double mutant in complex with ligand N
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL15A1 |
| Synchrotron site | NSRRC |
| Beamline | BL15A1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-08-02 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.319, 110.520, 127.779 |
| Unit cell angles | 90.00, 99.93, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.320 |
| R-factor | 0.21236 |
| Rwork | 0.210 |
| R-free | 0.26634 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ie4 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.196 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 25.000 | 25.000 | 2.400 |
| High resolution limit [Å] | 2.320 | 4.990 | 2.320 |
| Rmerge | 0.067 | 0.031 | 0.486 |
| Rmeas | 0.077 | 0.036 | 0.561 |
| Rpim | 0.038 | 0.017 | 0.276 |
| Total number of observations | 194860 | ||
| Number of reflections | 50048 | 5355 | 5058 |
| <I/σ(I)> | 12.6 | ||
| Completeness [%] | 95.0 | 99.9 | 96.6 |
| Redundancy | 3.9 | 4.2 | 3.8 |
| CC(1/2) | 0.998 | 0.803 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | 0.2M Ammonium Sulfate, 0.085M Sodium Cacodylate pH 6.5, 25-28%(w/v) Polyethylene Glycol 8000, 15%(v/v) Glycerol |
