1AHN
E. COLI FLAVODOXIN AT 2.6 ANGSTROMS RESOLUTION
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 140 |
| Detector technology | AREA DETECTOR |
| Collection date | 1995-10 |
| Detector | XUONG-HAMLIN MULTIWIRE |
| Spacegroup name | P 3 1 2 |
| Unit cell lengths | 78.830, 78.830, 52.070 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 10.000 - 2.600 |
| R-factor | 0.191 * |
| Rwork | 0.190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 25.000 * |
| Data reduction software | SDMS |
| Data scaling software | SDMS |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.760 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.064 * | 0.190 * |
| Total number of observations | 56473 * | |
| Number of reflections | 5995 | |
| <I/σ(I)> | 17.4 | 3.8 |
| Completeness [%] | 99.5 | 98.5 |
| Redundancy | 9.4 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 | 22 * | PROTEIN WAS CRYSTALLIZED IN 30% MPD, 100 MM CACL2, 200 MM PIPES BUFFER, PH 7.0, 295 K. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 7.5 (mg/ml) | |
| 2 | 1 | drop | MPD | 15 (%) | |
| 3 | 1 | drop | 50 (mM) | ||
| 4 | 1 | drop | PIPES | 100 (mM) | |
| 5 | 1 | reservoir | MPD | 30 (%) | |
| 6 | 1 | reservoir | 100 (mM) | ||
| 7 | 1 | reservoir | PIPES | 200 (mM) |
