2C74
14-3-3 Protein Eta (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 | 2005-10-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 75.731, 75.360, 113.529 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 62.990 - 2.700 |
| R-factor | 0.224 |
| Rwork | 0.220 |
| R-free | 0.29100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bq0 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.391 |
| 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] | 38.900 | 2.850 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.080 | 0.480 |
| Number of reflections | 18419 | |
| <I/σ(I)> | 12 | 2.4 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 3.5 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.6 | 0.1M CITRATE PH 5.6, 20% ISOPROPANOL, 20% PEG4000 |
