1AN7
RIBOSOMAL PROTEIN S8 FROM THERMUS THERMOPHILUS
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1996-02-10 |
Detector | MAR scanner 300 mm plate |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 67.860, 67.860, 174.090 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.900 |
R-factor | 0.162 |
Rwork | 0.162 |
R-free | 0.27500 |
Structure solution method | MIR |
RMSD bond length | 0.016 |
RMSD bond angle | 25.291 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.950 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.051 | 0.019 |
Number of reflections | 8932 | |
Completeness [%] | 94.5 | 93.6 |
Redundancy | 3.6 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 | 24 * | Tishchenko, S.V., (1997) Proteins: Struct.,Funct., Genet., 27, 309. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25-30 (mg/ml) | |
2 | 1 | drop | potassium phosphate | 40 (mM) | |
3 | 1 | drop | dithiothreitol | 1 (mM) | |
4 | 1 | reservoir | ammonium sulfate | 40 (%sat) | |
5 | 1 | reservoir | MPD | 7 (%(v/v)) |