1CGK
CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH NARINGENIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | MACSCIENCE |
Temperature [K] | 105 |
Detector technology | IMAGE PLATE |
Collection date | 1998-06 |
Detector | MAC Science DIP-2000 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 97.917, 97.917, 65.186 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 84.500 - 1.840 |
R-factor | 0.162 * |
Rwork | 0.161 |
R-free | 0.22500 |
Structure solution method | OTHER |
Starting model (for MR) | 1bi5 |
RMSD bond length | 0.013 |
RMSD bond angle | 2.419 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 ((ARPP)) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 51.680 | 1.890 |
High resolution limit [Å] | 1.840 | 1.840 |
Rmerge | 0.041 * | |
Number of reflections | 26948 | |
<I/σ(I)> | 13.7 | 7.5 |
Completeness [%] | 86.6 | 8.3 |
Redundancy | 2.8 | 0.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.5 | 4 * | THE DROPLE CONSISTED ON 25 MGR/ML (FINAL CONCENTRATION) PROTEIN MIXED WITH THE RESERVOIR WHICH CONTAINED 2.4 M AMMONIUM SULFATE, 100 MM PIPES BUFFER (PH 6.5) , IN THE PRESENCE (UP TO 5 MM) OR ABSENCE OF DTT REDUCING AGENT. CRYSTALS WERE STABILIZED IN 40% (V/V) PEG400, 100 MM PIPES 16 MM NARINGENIN PRIOR TO FREEZING AT 105 K, pH 6.50 |
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) |