1F5V
STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS. ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE AMINO ACID SUBSTITUTION
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 1 |
Unit cell lengths | 51.560, 52.860, 52.830 |
Unit cell angles | 75.79, 60.71, 61.17 |
Refinement procedure
Resolution | 7.000 - 1.700 |
R-factor | 0.189 * |
Rwork | 0.189 |
R-free | 0.20600 |
RMSD bond length | 0.011 |
RMSD bond angle | 21.918 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | |
High resolution limit [Å] | 1.700 * |
Rmerge | 0.033 * |
Number of reflections | 41935 * |
Completeness [%] | 91.8 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | 5 * | PEG 6000, MES, sodium hydroxide, PEG 400, dioxane, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 281.0K |
1 | Vapor diffusion, hanging drop * | 6.5 | 5 * | PEG 6000, MES, sodium hydroxide, PEG 400, dioxane, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 281.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG6000 | 22.5 (%) | |
2 | 1 | reservoir | PEG400 | 2-15 (%) | |
3 | 1 | reservoir | MES | 100 (mM) | |
4 | 1 | drop | protein | 9 (mg/ml) |