3WEK
Crystal structure of the human squalene synthase F288L 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 | 2012-09-17 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 94.192, 106.502, 32.988 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.600 - 1.850 |
| R-factor | 0.22714 |
| Rwork | 0.225 |
| R-free | 0.25711 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3vj8 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.411 |
| 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 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.086 | 0.499 |
| Number of reflections | 29252 | |
| <I/σ(I)> | 16.7 | 2 |
| Completeness [%] | 99.8 | 99.5 |
| Redundancy | 5 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 20% PEG 4000, 10% 2-propanol, 0.1M HEPES, 1mM presqualene pyrophosphate, 1mM MgCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
