2BTP
14-3-3 Protein Theta (Human) Complexed to Peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-05-21 |
| Detector | RIGAKU-MSC R-AXIS HTC |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.307, 85.964, 64.666 |
| Unit cell angles | 90.00, 112.67, 90.00 |
Refinement procedure
| Resolution | 59.660 - 2.800 |
| R-factor | 0.21 |
| Rwork | 0.206 |
| R-free | 0.25900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qja |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.404 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.880 | 2.950 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.090 | 0.410 |
| Number of reflections | 14743 | |
| <I/σ(I)> | 17.7 | 3.5 |
| Completeness [%] | 96.4 | 93.3 |
| Redundancy | 6.3 | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 0.2M SODIUM ACETATE TRIHYDRATE, 0.1M TRISHCL PH8.5,30% PEG4000, pH 8.50 |
