1JW4
Structure of ligand-free maltodextrin-binding protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 200 |
Detector technology | IMAGE PLATE |
Collection date | 1999-11-08 |
Detector | MACSCIENCE |
Spacegroup name | P 1 |
Unit cell lengths | 38.100, 44.600, 58.300 |
Unit cell angles | 99.60, 101.60, 104.50 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.2 * |
Rwork | 0.200 |
R-free | 0.26000 |
RMSD bond length | 0.010 * |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 1.970 |
High resolution limit [Å] | 2.000 * | 1.900 |
Rmerge | 0.043 | 0.165 |
Number of reflections | 24467 | |
<I/σ(I)> | 16 | |
Completeness [%] | 87.7 | 57.9 |
Redundancy | 1.6 * | 1.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.6 * | 298 | PEG 20k, Mes, sodium azide, pH 6.2, VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | MBP | 3.5 (mg/ml) | |
2 | 1 | drop | maltotetraitol | 1 (mM) | |
3 | 1 | drop | PEG3350 | 20 (%) | pH6.6 |
4 | 1 | reservoir | PEG3350 | 30 (%) |