3DE0
Proteinase K by LB nanotemplate method after the second step of 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 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-07-02 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97625 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 67.664, 67.664, 101.622 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.830 - 1.900 |
| R-factor | 0.19 |
| Rwork | 0.188 |
| R-free | 0.23000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ddz |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.305 |
| 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] | 56.344 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.131 | 0.293 |
| Total number of observations | 12851 | |
| Number of reflections | 17199 | |
| <I/σ(I)> | 4.4 | 1.8 |
| Completeness [%] | 89.9 | 89.3 |
| Redundancy | 5 | 5.2 |
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 microL of protein solution with 4 microL of reservoir solution., VAPOR DIFFUSION, HANGING DROP, temperature 293K |
