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 |