5IE4
Crystal structure of a lactonase mutant in complex with substrate a
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-06-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97622 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 86.205, 86.205, 473.247 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 25.000 - 2.800 |
| R-factor | 0.2063 |
| Rwork | 0.203 |
| R-free | 0.26483 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wzl |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.500 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 25.000 | 25.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 6.010 | 2.800 |
| Rmerge | 0.053 | 0.026 | 0.163 |
| Rmeas | 0.059 | ||
| Rpim | 0.024 | ||
| Total number of observations | 162671 | ||
| Number of reflections | 26370 | ||
| <I/σ(I)> | 13.9 | ||
| Completeness [%] | 97.5 | 92.9 | 98.9 |
| Redundancy | 6.2 | 5.5 | 6.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | 24% PEG 2000 MME, 0.1M Bis-Tris |
