1RQI
Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Dimethylallyl S-Thiolodiphosphate
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 | 88.839, 88.839, 174.769 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 * - 2.420 |
R-factor | 0.20604 |
Rwork | 0.203 |
R-free | 0.26000 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 1.742 |
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 | 2.510 |
High resolution limit [Å] | 2.420 | 2.420 |
Rmerge | 0.100 * | 0.443 * |
Total number of observations | 194920 * | |
Number of reflections | 26473 | |
<I/σ(I)> | 15.9 | 3.2 |
Completeness [%] | 96.1 | 93.2 |
Redundancy | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 6 | 298 | Hosfield, D., (2003) J. Struct. Biol., 142, 207. * |