4OW3
Thermolysin structure determined by free-electron laser
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | FREE ELECTRON LASER |
Source details | SLAC LCLS BEAMLINE CXI |
Synchrotron site | SLAC LCLS |
Beamline | CXI |
Temperature [K] | 298 |
Detector technology | PIXEL |
Collection date | 2011-12-01 |
Detector | CS-PAD detector |
Wavelength(s) | 1.269, 1.297 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 92.893, 92.893, 130.438 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 68.472 - 2.100 |
R-factor | 0.219654161884 |
Rwork | 0.217 |
R-free | 0.26317 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2tli |
RMSD bond length | 0.003 |
RMSD bond angle | 0.682 |
Refinement software | PHENIX ((phenix.refine: dev_1549+SVN)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 68.500 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 19861 | |
<I/σ(I)> | 50.2 | 5.6 |
Completeness [%] | 99.1 | 91.2 |
Redundancy | 209 | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 6.5 | 298 | 300 ul of the protein stock was mixed in a 1:1 ratio with 40% PEG 2000, 100 mM MES pH 6.5, 5 mM CaCl2. Crystallization occurred within minutes. |