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 |