4N9U
The role of lysine 200 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 | 2009-09-15 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9796 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 111.110, 111.110, 69.580 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.690 - 2.110 |
| R-factor | 0.1935 |
| Rwork | 0.191 |
| R-free | 0.24020 |
| 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 (2.10.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.090 | 2.200 |
| High resolution limit [Å] | 2.110 | 2.110 |
| Rmerge | 0.091 | |
| Number of reflections | 25619 | |
| <I/σ(I)> | 14.7 | |
| Completeness [%] | 99.8 | 80.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.2 M NH4CL, PEG6000, 10% Ethylene Glycol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
