1BS0
PLP-DEPENDENT ACYL-COA SYNTHASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-06-15 |
Detector | MARRESEARCH |
Spacegroup name | P 31 1 2 |
Unit cell lengths | 58.520, 58.520, 194.640 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 1.650 |
R-factor | 0.1779 |
R-free | 0.21240 |
Structure solution method | MIR |
RMSD bond length | 0.022 |
RMSD bond angle | 0.026 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.680 |
High resolution limit [Å] | 1.640 | 1.650 |
Rmerge | 0.084 | 0.369 |
Number of reflections | 46252 | |
<I/σ(I)> | 31.3 | 3.3 |
Completeness [%] | 100.0 | 99.6 * |
Redundancy | 14.3 | 8.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.9 | PROTEIN WAS CRYSTALLIZED FROM 0.2M AMMONIUM SULPHATE, 200MM BIS-TRIS,, pH 7.9 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 1.6 (M) | |
3 | 1 | reservoir | Bis-Tris-propane | 200 (mM) |