5G2G
Crystal structure of ketosteroid isomerase containing M116K mutation in the equilenin-bound form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 5C (4A) |
| Synchrotron site | PAL/PLS |
| Beamline | 5C (4A) |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 35.525, 73.582, 95.214 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.971 - 1.599 |
| R-factor | 0.1997 |
| Rwork | 0.198 |
| R-free | 0.22970 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4k1u |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.057 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.630 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.070 | 0.330 |
| Number of reflections | 33850 | |
| <I/σ(I)> | 36.37 | 2.86 |
| Completeness [%] | 99.1 | 94.2 |
| Redundancy | 8.6 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | BIS-TRIS, MAGNESIUM CHLORIDE, PEG 3350, PH 5.50 |
