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 |
