5XFY
Crystal structure of a novel PET hydrolase S131A mutant from Ideonella sakaiensis 201-F6
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 | 2016-12-27 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 114.185, 50.331, 40.979 |
| Unit cell angles | 90.00, 92.24, 90.00 |
Refinement procedure
| Resolution | 25.000 - 1.400 |
| R-factor | 0.1355 |
| Rwork | 0.134 |
| R-free | 0.15890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4wfi |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.501 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 25.000 | 25.000 | 1.450 |
| High resolution limit [Å] | 1.400 | 3.013 | 1.400 |
| Rmerge | 0.036 | 0.027 | 0.207 |
| Rmeas | 0.040 | 0.030 | 0.228 |
| Rpim | 0.016 | 0.013 | 0.094 |
| Total number of observations | 261939 | ||
| Number of reflections | 45597 | ||
| <I/σ(I)> | 24.9 | ||
| Completeness [%] | 99.7 | 97.2 | 100 |
| Redundancy | 5.7 | 5.6 | 5.8 |
| CC(1/2) | 0.999 | 0.977 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | Ammonium Sulfate, NaCl, Bis-Tris |
