1A38
14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-10 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 65 |
Unit cell lengths | 95.520, 95.520, 235.360 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 3.350 |
R-factor | 0.3 * |
Rwork | 0.330 |
R-free | 0.35000 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.020 * |
RMSD bond angle | 2.700 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.8) |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.500 |
High resolution limit [Å] | 3.350 | 3.350 |
Rmerge | 0.060 * | 0.320 |
Number of reflections | 17105 | |
<I/σ(I)> | 18.5 | 4.9 |
Completeness [%] | 96.7 | 91.6 |
Redundancy | 3.4 | 3.15 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | 4 * | Liu, D., (1995) Nature, 376, 191. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5-10 (mg/ml) | |
2 | 1 | reservoir | PEG3500 | 20-24 (%) | |
3 | 1 | reservoir | Tris-HCl | 100 (mM) | |
4 | 1 | reservoir | 10 (mM) | ||
5 | 1 | reservoir | 1 (mM) |