5XFZ
Crystal structure of a novel PET hydrolase R103G/S131A mutant from Ideonella sakaiensis 201-F6
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13C1 |
| Synchrotron site | NSRRC |
| Beamline | BL13C1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-03-18 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97622 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.945, 51.618, 84.590 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 - 1.550 |
| R-factor | 0.1401 |
| Rwork | 0.139 |
| R-free | 0.16950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4wfi |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.502 |
| 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 | 1.610 |
| High resolution limit [Å] | 1.550 | 3.340 | 1.550 |
| Rmerge | 0.076 | 0.031 | 0.491 |
| Rmeas | 0.086 | 0.035 | 0.555 |
| Rpim | 0.039 | 0.016 | 0.255 |
| Total number of observations | 157183 | ||
| Number of reflections | 33154 | ||
| <I/σ(I)> | 7.7 | ||
| Completeness [%] | 99.9 | 99.5 | 99.9 |
| Redundancy | 4.7 | 4.6 | 4.6 |
| CC(1/2) | 0.999 | 0.859 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | Ammonium Sulfate, NaCl, HEPES |
