1B3S
STRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX7.2 |
| Synchrotron site | SRS |
| Beamline | PX7.2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-11 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 201.900, 43.900, 83.400 |
| Unit cell angles | 90.00, 110.70, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.390 |
| R-factor | 0.247 * |
| Rwork | 0.247 |
| R-free | 0.32400 |
| Structure solution method | OTHER |
| Starting model (for MR) | 1brs |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.023 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | X-PLOR |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.925 | 2.520 |
| High resolution limit [Å] | 2.391 | 2.390 |
| Rmerge | 0.098 | 0.242 |
| Number of reflections | 26773 | |
| <I/σ(I)> | 9.42 | 2.51 |
| Completeness [%] | 96.2 | 90 |
| Redundancy | 3.2 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | 0.2M (NH4)2SO4; 0.1M TRIS/HCL PH 8.0: 22% PEG-8000 |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | PEG 8000 | ||
| 2 | 1 | 1 | TRIS_HCL | ||
| 3 | 1 | 1 | NH4 SULFATE |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG8000 | 18-24 (%(w/v)) | |
| 2 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
| 3 | 1 | reservoir | Tris | 0.1 (M) | |
| 4 | 1 | drop | protein | 20 (mg/ml) |
