3DVS
Proteinase K by LB nanotmplate method after the second step of high 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 | 2007-06-14 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.933 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 67.986, 67.986, 102.248 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 56.610 - 1.020 |
| R-factor | 0.22 |
| Rwork | 0.220 |
| R-free | 0.22400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ptk |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.120 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.25) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.614 | 1.080 |
| High resolution limit [Å] | 1.020 | 1.020 |
| Rmerge | 0.056 | 0.534 |
| Total number of observations | 8026 | |
| Number of reflections | 98762 | |
| <I/σ(I)> | 7.9 | 1.4 |
| Completeness [%] | 82.0 | 29.4 |
| Redundancy | 5.4 | 1.6 |
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 |
