1B43
FEN-1 FROM P. FURIOSUS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-1 |
Synchrotron site | SSRL |
Beamline | BL9-1 |
Temperature [K] | 100 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 115.820, 122.040, 134.420 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.231 |
Rwork | 0.231 |
R-free | 0.27900 |
Structure solution method | MIRAS |
RMSD bond length | 0.008 |
RMSD bond angle | 1.420 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASES |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.038 * | 0.346 * |
Total number of observations | 208396 * | |
Number of reflections | 62063 | |
<I/σ(I)> | 15 | 3 |
Completeness [%] | 96.0 | 88.3 |
Redundancy | 3.4 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | drop consists of equal volume of protein and precipitant solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protease | 100 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 60 (%sat) | precipitant |
3 | 1 | reservoir | 50 (mM) | precipitant | |
4 | 1 | reservoir | imidazole/malate | 100 (mM) | precipitant |