6KKF
Crystal structure of proteinase K complexed with a triglycine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 11C |
| Synchrotron site | PAL/PLS |
| Beamline | 11C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-09-27 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.9796 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.512, 67.685, 43.592 |
| Unit cell angles | 90.00, 111.39, 90.00 |
Refinement procedure
| Resolution | 40.590 - 1.400 |
| R-factor | 0.184 |
| Rwork | 0.182 |
| R-free | 0.21810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ic6 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.993 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.420 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.166 | 0.529 |
| Rpim | 0.096 | 0.313 |
| Number of reflections | 38738 | 1831 |
| <I/σ(I)> | 25.65 | 5.17 |
| Completeness [%] | 94.8 | 89.4 |
| Redundancy | 3.8 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291.5 | Tris-HCl, ammonium sulfate |
