3DDZ
Proteinase K by LB nanotemplate method after the first 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 | 67.693, 67.693, 101.658 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.850 - 1.700 |
R-factor | 0.198 |
Rwork | 0.196 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3d9q |
RMSD bond length | 0.009 |
RMSD bond angle | 1.214 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (3.2.25) |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.790 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.122 | 0.335 |
Total number of observations | 9568 | |
Number of reflections | 23245 | |
<I/σ(I)> | 4.7 | 1.5 |
Completeness [%] | 87.6 | 76.8 |
Redundancy | 4.6 | 3.3 |
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. 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 |