4NG6
The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 111.740, 111.740, 66.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.980 - 2.350 |
R-factor | 0.1803 |
Rwork | 0.178 |
R-free | 0.23000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3cp6 |
RMSD bond length | 0.010 |
RMSD bond angle | 0.980 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | BUSTER (2.10.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 33.980 | 2.490 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.161 | |
Number of reflections | 17960 | |
<I/σ(I)> | 10.3 | |
Completeness [%] | 99.2 | 95.7 |
Redundancy | 8.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.2 M NH4CL, PEG 6000, 10% Ethylene Glycol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |