1RQJ
Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Risedronate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 97 |
| Detector technology | CCD |
| Collection date | 2002-11-11 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 41 2 2 |
| Unit cell lengths | 88.800, 88.800, 174.988 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.950 |
| R-factor | 0.20729 |
| Rwork | 0.206 |
| R-free | 0.24000 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.230 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.077 * | 0.516 * |
| Total number of observations | 396530 * | |
| Number of reflections | 51703 | |
| <I/σ(I)> | 27.8 | 3 |
| Completeness [%] | 99.3 | 96.2 |
| Redundancy | 7.66 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 6.5 | 298 | Hosfield, D., (2003) J. Struct. Biol., 142, 207. * |
