1HFX
ALPHA-LACTALBUMIN
Experimental procedure
| Temperature [K] | 298 |
| Collection date | 1992-02-01 |
| Detector | SIEMENS |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 32.590, 64.870, 49.000 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.900 |
| R-factor | 0.179 |
| Rwork | 0.179 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | HUMAN ALPHA-LACTALBUMIN |
| RMSD bond length | 0.009 |
| RMSD bond angle | 22.950 * |
| Data reduction software | XENGEN |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 39.100 |
| High resolution limit [Å] | 1.900 |
| Rmerge | 0.083 |
| Number of reflections | 8003 |
| Completeness [%] | 88.0 |
| Redundancy | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4.6 | 20 * | 0.2M AMMONIUM SULFATE, 20-25% (W/V) PEG 4000, 0.1M SODIUM ACETATE PH4.6, 20MG/ML PROTEIN 20 DEGREES C, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | ammonium salfate | 0.2 (M) | |
| 2 | 1 | reservoir | PEG4000 | 20-25 (%) | |
| 3 | 1 | reservoir | 0.1 (M) | ||
| 4 | 1 | drop | protein | 20 (mg/ml) |
