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) |