3D9Q
Proteinase K by LB nanotemplate method before high X-Ray dose on ESRF ID23-1 beamline
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Detector technology | CCD |
| Collection date | 2007-07-02 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.97625 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 67.760, 67.760, 101.609 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.650 - 1.430 |
| R-factor | 0.213 |
| Rwork | 0.211 |
| R-free | 0.24100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ptk |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.126 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.25) |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.375 | 1.500 |
| High resolution limit [Å] | 1.426 | 1.430 |
| Rmerge | 0.115 | 0.485 |
| Total number of observations | 1690 | |
| Number of reflections | 32221 | |
| <I/σ(I)> | 4.8 | 1.3 |
| Completeness [%] | 72.2 | 21.4 |
| Redundancy | 4.2 | 1.3 |
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, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
