4Q23
The role of threonine 201 and tyrosine 204 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I02 |
Synchrotron site | Diamond |
Beamline | I02 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-05-15 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9796 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 111.360, 111.360, 67.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.020 - 1.980 |
R-factor | 0.1931 |
Rwork | 0.192 |
R-free | 0.22290 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3cp6 |
RMSD bond length | 0.010 |
RMSD bond angle | 0.930 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | BUSTER (2.8.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.020 | 2.050 |
High resolution limit [Å] | 1.980 | 1.980 |
Number of reflections | 29838 | |
Completeness [%] | 99.3 | 99.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.2M NH4Cl, 20% PEG 6000, 10% Glycol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |