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 |