3I2Y
Proteinase K by Classical hanging drop Method before high X-Ray dose on ID14-2 Beamline at ESRF
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-05-14 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.2 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 67.943, 67.943, 102.378 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.130 - 0.995 |
| R-factor | 0.201 |
| Rwork | 0.200 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ptk |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.068 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.25) |
| Phasing software | REFMAC |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.614 | 1.050 |
| High resolution limit [Å] | 0.994 | 0.990 |
| Rmerge | 0.092 | 0.763 |
| Total number of observations | 10276 | |
| Number of reflections | 114135 | |
| <I/σ(I)> | 14 | 1 |
| Completeness [%] | 86.4 | 36.2 |
| Redundancy | 5.8 | 1.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 20mg/mL in 25mM HEPES, pH7.0 PMSF, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
