7CY0
Crystal structure of S185H mutant PET hydrolase from Ideonella sakaiensis
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 | 2019-10-29 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.925, 51.806, 84.287 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.710 - 1.320 |
| R-factor | 0.1451 |
| Rwork | 0.144 |
| R-free | 0.16560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5xg0 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.495 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0266) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 25.000 | 25.000 | 1.370 |
| High resolution limit [Å] | 1.320 | 2.840 | 1.320 |
| Rmerge | 0.045 | 0.028 | 0.438 |
| Rmeas | 0.049 | 0.031 | 0.473 |
| Rpim | 0.018 | 0.011 | 0.176 |
| Total number of observations | 360092 | ||
| Number of reflections | 51200 | 5513 | 4970 |
| <I/σ(I)> | 14 | ||
| Completeness [%] | 96.7 | 98.6 | 95.5 |
| Redundancy | 7 | 7 | 7 |
| CC(1/2) | 0.999 | 0.933 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 298 | Polyethylene Glycol 6000, Glycerol, MES |
