1F8N
LIPOXYGENASE-1 (SOYBEAN) AT 100K, NEW REFINEMENT
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1994-02-01 |
Detector | CUSTOM-MADE |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 94.900, 94.000, 49.900 |
Unit cell angles | 90.00, 90.10, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.400 |
R-factor | 0.198 * |
Rwork | 0.198 |
R-free | 0.21200 |
Structure solution method | MIR |
RMSD bond length | 0.010 |
RMSD bond angle | 1.430 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.420 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.037 | 0.343 |
Number of reflections | 161029 | |
<I/σ(I)> | 35.7 | |
Completeness [%] | 96.0 | 91.6 |
Redundancy | 6.8 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.6 * | 21 * | Minor, W., (1996) Biochemistry, 35, 10687. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | acetate | 0.1 (M) | |
2 | 1 | drop | PEG3400 | 4 (%(w/v)) | |
3 | 1 | drop | protein | 4 (mg/ml) | |
4 | 1 | reservoir | PEG3350 | 9 (%) | |
5 | 1 | reservoir | sodium acetate | 0.2 (M) |