3WEJ
Crystal structure of the human squalene synthase F288A mutant in complex with presqualene pyrophosphate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-18 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 35.714, 94.503, 105.314 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.040 - 2.000 |
| R-factor | 0.21115 |
| Rwork | 0.208 |
| R-free | 0.27580 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3vj8 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.419 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.092 | 0.520 |
| Number of reflections | 24564 | |
| <I/σ(I)> | 18.5 | 3 |
| Completeness [%] | 99.4 | 99.6 |
| Redundancy | 4.6 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 20% PEG 2000 MME, 0.01 M NiCl2, 0.1M Tris, 1mM presqualene pyrophosphate, 1mM MgCl2, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
