5FKY
Structure of a hydrolase bound with an inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 1 |
| Unit cell lengths | 51.440, 93.690, 99.020 |
| Unit cell angles | 104.07, 94.18, 102.97 |
Refinement procedure
| Resolution | 95.170 - 1.800 |
| R-factor | 0.21299 |
| Rwork | 0.211 |
| R-free | 0.24855 |
| Structure solution method | OTHER |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.698 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.800 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.080 | 0.420 |
| Number of reflections | 153821 | |
| <I/σ(I)> | 9.4 | 1.9 |
| Completeness [%] | 95.8 | 91.9 |
| Redundancy | 2 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
