7SH6
Crystal structure of a PET hydrolase mutant from Ideonella Sakaiensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-09-19 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.03317 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.942, 51.182, 84.047 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.710 - 1.440 |
| R-factor | 0.1583 |
| Rwork | 0.158 |
| R-free | 0.16780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6ij6 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.865 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.18rc3_3805) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.460 |
| High resolution limit [Å] | 1.440 | 3.910 | 1.440 |
| Rmerge | 0.074 | 0.066 | 0.195 |
| Rmeas | 0.080 | 0.073 | 0.228 |
| Rpim | 0.031 | 0.031 | 0.113 |
| Total number of observations | 267933 | ||
| Number of reflections | 40349 | 2191 | 1901 |
| <I/σ(I)> | 8.8 | ||
| Completeness [%] | 99.4 | 98.9 | 94.3 |
| Redundancy | 6.6 | 5.6 | 3.5 |
| CC(1/2) | 0.992 | 0.948 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 0.1M bis-TRIS pH 5.5, 2.0M Ammonium Sulfate |
