1EFP
ELECTRON TRANSFER FLAVOPROTEIN (ETF) FROM PARACOCCUS DENITRIFICANS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 297 |
Detector technology | IMAGE PLATE |
Collection date | 1995-01 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 70.430, 80.530, 183.970 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 12.000 - 2.600 |
R-factor | 0.193 |
Rwork | 0.193 |
R-free | 0.28600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1efv |
RMSD bond length | 0.007 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 2.600 |
Rmerge | 0.054 |
Total number of observations | 118452 * |
Number of reflections | 28666 |
Completeness [%] | 87.8 |
Redundancy | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.8 | 19 * | 18% PEG 8000, 25 MM KH2PO4, 100 UM FAD, AND 5 MM MGCL2, FINAL PH = 5.8. THE PROTEIN WAS MIXED WITH SOLUTION IN A 1:1 RATIO (PROTEIN WAS IN 10 MM TRIS, PH 7.4). |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12 (mg/ml) | |
2 | 1 | reservoir | PEG8000 | 18 (%(w/v)) | |
3 | 1 | reservoir | potassium phosphate | 25 (mM) | |
4 | 1 | reservoir | FAD | 0.100 (mM) | |
5 | 1 | reservoir | 5 (mM) |