7DZU
Cyrstal structure of PETase K169A mutant from Rhizobacter gummiphilus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 7A (6B, 6C1) |
| Synchrotron site | PAL/PLS |
| Beamline | 7A (6B, 6C1) |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2020-12-17 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.139, 54.106, 110.136 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.070 - 2.400 |
| R-factor | 0.1865 |
| Rwork | 0.183 |
| R-free | 0.25260 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7dzt |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.620 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 6.510 | 2.400 |
| Rmerge | 0.113 | 0.064 | 0.414 |
| Rmeas | 0.124 | 0.072 | 0.451 |
| Rpim | 0.051 | 0.031 | 0.176 |
| Total number of observations | 71359 | ||
| Number of reflections | 12259 | 693 | 593 |
| <I/σ(I)> | 11.6 | ||
| Completeness [%] | 98.1 | 97.3 | 98.3 |
| Redundancy | 5.8 | 5.1 | 6.3 |
| CC(1/2) | 0.995 | 0.933 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7.5 | 298 | NaCl, HEPES |
