3DE4
Proteinase K by Classical hanging drop 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 | 2007-02-07 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97625 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 67.847, 67.847, 102.482 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.020 - 1.800 |
R-factor | 0.184 |
Rwork | 0.182 |
R-free | 0.21800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 1.358 |
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 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.099 | 0.457 |
Total number of observations | 14026 | |
Number of reflections | 22616 | |
<I/σ(I)> | 6.6 | 1.6 |
Completeness [%] | 99.2 | 98 |
Redundancy | 4.7 | 4.4 |
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 |