2BR9
14-3-3 Protein Epsilon (Human) Complexed to Peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-04-23 |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 78.011, 81.533, 80.966 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 56.340 - 1.750 |
| R-factor | 0.19 |
| Rwork | 0.188 |
| R-free | 0.23900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1o9d |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.644 |
| 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] | 36.420 | 1.840 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.090 | 0.640 |
| Number of reflections | 138812 | |
| <I/σ(I)> | 16.1 | 1.9 |
| Completeness [%] | 99.2 | 97.4 |
| Redundancy | 5.3 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 40% MPD, 5% PEG10000, 0.1M CACODYLATE PH6.5. PROTEIN IN 150MM NACL, 50MM TRIS PH8, pH 8.00 |
