1RH2
RECOMBINANT HUMAN INTERFERON-ALPHA 2B
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 103 |
Detector technology | IMAGE PLATE |
Collection date | 1995-12 |
Detector | RIGAKU |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 62.400, 75.500, 148.200 |
Unit cell angles | 90.00, 90.80, 90.00 |
Refinement procedure
Resolution | 6.000 - 2.900 |
R-factor | 0.227 |
Rwork | 0.227 |
R-free | 0.31100 |
Structure solution method | MULTIPLE ISOMORPHOUS REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 21.400 * |
Data reduction software | MOLECULAR (STRUCTURE CORP.) |
Data scaling software | MSC |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 6.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.095 | 0.240 |
Total number of observations | 217393 * | |
Number of reflections | 31925 | |
<I/σ(I)> | 10 | 3.2 |
Completeness [%] | 96.0 | 92 |
Redundancy | 6.8 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.6 | 23 * | PROTEIN WAS CRYSTALLIZED FROM 40MM ZINC ACETATE, 30MM CACODYLATE, PH 5.6; MACRO SEEDING WAS PERFORMED TO GET REASONABLE SIZE CRYSTALS., macroseeding |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 40 (mg/ml) | |
2 | 1 | reservoir | 40 (mM) | ||
3 | 1 | reservoir | cacodylate | 30 (mM) |