1FQA
STRUCTURE OF MALTOTETRAITOL BOUND TO OPEN-FORM MALTODEXTRIN BINDING PROTEIN IN P2(1)CRYSTAL FORM
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 200 |
Detector technology | IMAGE PLATE |
Detector | MACSCIENCE |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 43.900, 65.800, 57.800 |
Unit cell angles | 90.00, 101.20, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.900 |
R-factor | 0.176 * |
Rwork | 0.176 |
R-free | 0.21500 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.045 | 0.126 |
Total number of observations | 170555 * | |
Number of reflections | 21890 | |
Completeness [%] | 84.0 | 69.6 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.2 * | 273 | PEG 3350, NaN3, MES, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 273.0K |
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 (%) | |
4 | 1 | drop | sodium azide | 0.02 (%(w/v)) | |
5 | 1 | drop | MES | 10 (mM) | |
6 | 1 | drop | protein | 12 (mg/ml) | |
7 | 1 | reservoir | PEG3350 | 30 (%) | |
8 | 1 | reservoir | sodium azide | 0.02 (%(w/v)) | |
9 | 1 | reservoir | MES | 10 (mM) |