1E1N
Structure of adrenodoxin reductase at 2.4 Angstrom in crystal form A'
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 100 |
Collection date | 1998-01-15 |
Detector | SIEMENS |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 57.800, 62.000, 83.000 |
Unit cell angles | 90.00, 107.10, 90.00 |
Refinement procedure
Resolution | 29.000 - 2.400 |
Rwork | 0.201 |
R-free | 0.26500 |
Structure solution method | MAD |
RMSD bond length | 0.012 |
RMSD bond angle | 0.027 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 32.300 | 2.480 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.057 | 0.170 |
Number of reflections | 17479 | |
<I/σ(I)> | 11.4 | 5 |
Completeness [%] | 74.4 | 36.8 |
Redundancy | 2.4 | 1.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | 20 * | pH 6.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 4 (mg/ml) | |
2 | 1 | drop | glycerol | 5 (%) | |
3 | 1 | drop | PEG8000 | 8 (%(w/v)) | |
4 | 1 | drop | sodium cacodylate | 50 (mM) | Buffer C |
5 | 1 | drop | calcium acetate | 100 (mM) | BufferC |
6 | 1 | reservoir | Buffer C | ||
7 | 1 | reservoir | PEG8000 | 12 (%(w/v)) |