1JWX
Chalcone Synthase--F215S mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-01-11 |
Detector | MARRESEARCH |
Wavelength(s) | 1.08 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 97.805, 97.805, 65.726 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 26.000 - 1.630 |
R-factor | 0.2 |
Rwork | 0.190 |
R-free | 0.22500 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | wild-type CHS with Phe215 mutated to alanine |
RMSD bond length | 0.013 |
RMSD bond angle | 2.100 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 26.000 | 1.670 |
High resolution limit [Å] | 1.630 | 1.620 |
Rmerge | 0.035 * | 0.120 * |
Total number of observations | 226775 * | |
Number of reflections | 43804 | |
<I/σ(I)> | 27.5 | 6.1 |
Completeness [%] | 95.9 | 81.6 |
Redundancy | 5.2 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.5 | 4 * | Ferrer, J.L., (1999) Nature Struct. Biol., 6, 775. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 2.2-2.4 (M) | |
3 | 1 | reservoir | PIPES | 0.1 (M) |