3DWE
Proteinase K by Classical hanging drop method after high X-Ray dose on ESRF ID14-2 beamline
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 110 |
| 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 | 67.948, 67.948, 102.388 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.060 - 0.990 |
| R-factor | 0.221 |
| Rwork | 0.221 |
| R-free | 0.22200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ptk |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.087 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.25) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.615 | 1.050 |
| High resolution limit [Å] | 0.990 | 0.990 |
| Rmerge | 0.090 | 0.768 |
| Total number of observations | 9862 | |
| Number of reflections | 114171 | |
| <I/σ(I)> | 5.6 | 0.9 |
| Completeness [%] | 86.1 | 35 |
| Redundancy | 5.8 | 1.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 20mg/ml of protein in 25mM HEPES pH7.0, reservoir solution composed by 25mM HEPES and 400mM Na/K tartrate at pH7.0. Onto the siliconized glass cover slides were mixed 4 microlitres of protein solution with 4 microlitres of reservoir solution., VAPOR DIFFUSION, HANGING DROP, temperature 293K |
