4B5L
The 1.6 A High Energy Room Temperature Structure of Proteinase K at 38.4 keV and 0.04 MGy
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID15C |
| Synchrotron site | ESRF |
| Beamline | ID15C |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 2011-11-28 |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 68.538, 68.538, 108.375 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.980 - 1.600 |
| R-factor | 0.15952 |
| Rwork | 0.158 |
| R-free | 0.18435 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3q5g |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.460 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 11.000 | 1.630 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.130 | 0.820 |
| Number of reflections | 34541 | |
| <I/σ(I)> | 11.1 | 1.5 |
| Completeness [%] | 99.5 | 99.6 |
| Redundancy | 5.9 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 1 UL OF 40 MG/ML PROTEIN IN DH2O MIXED WITH 1 MUL OF THE MOTHER LIQUOR. MOTHER LIQUOR 400 MM AMMONIUM SO4, 25% GLYCEROL, 100 MM NA CACODYLATE PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K |
