5L1S
X-ray Structure of F232L mutant of Cytochrome P450 PntM with pentalenolactone F
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-10-31 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 44.595, 164.145, 82.535 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.600 - 2.080 |
R-factor | 0.1561 |
Rwork | 0.154 |
R-free | 0.19310 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2x9p |
RMSD bond length | 0.008 |
RMSD bond angle | 0.976 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.15) |
Phasing software | PHASER |
Refinement software | PHENIX (1.10pre_2131) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 45.600 | 45.600 | 2.130 |
High resolution limit [Å] | 2.080 | 9.050 | 2.080 |
Rmerge | 0.153 | 0.045 | 0.550 |
Rmeas | 0.166 | ||
Rpim | 0.062 | ||
Total number of observations | 262065 | ||
Number of reflections | 37071 | ||
<I/σ(I)> | 11 | ||
Completeness [%] | 98.6 | 99.6 | 92.1 |
Redundancy | 7.1 | 6.2 | 4.8 |
CC(1/2) | 0.993 | 0.998 | 0.724 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 9 | 288 | Bicine, sodium citrate, glycerol |