1B2S
STRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-10-15 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 206.240, 43.510, 83.690 |
| Unit cell angles | 90.00, 107.42, 90.00 |
Refinement procedure
| Resolution | 31.000 - 1.820 |
| R-factor | 0.193 * |
| Rwork | 0.194 |
| R-free | 0.24800 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1brs |
| RMSD bond length | 0.012 |
| RMSD bond angle | 0.028 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.710 | 1.910 |
| High resolution limit [Å] | 1.820 | 1.820 |
| Rmerge | 0.071 | 0.238 |
| Number of reflections | 59006 | |
| <I/σ(I)> | 7.2 | 3.2 |
| Completeness [%] | 91.5 | 80.9 |
| Redundancy | 3.5 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | 18% PEG-4K 0.1M TRIS PH8.0 0.2M LI2SO4 |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | PEG 4000 | ||
| 2 | 1 | 1 | TRIS | ||
| 3 | 1 | 1 | LI SULFATE |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG4000 | 20-24 (%(w/v)) | |
| 2 | 1 | reservoir | 0.2 (M) | ||
| 3 | 1 | reservoir | Tris | 0.1 (M) | |
| 4 | 1 | drop | protein | 20 (mg/ml) |
