3MXC
Structures of Grb2-SH2 Domain and AICD peptide Complexes Reveal a Conformational Switch and Their Functional Implications.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | BRUKER AXS MICROSTAR |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-07-02 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 59.369, 59.369, 117.101 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.690 - 2.000 |
R-factor | 0.217 |
Rwork | 0.217 |
R-free | 0.24400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jyr |
RMSD bond length | 0.015 |
RMSD bond angle | 1.600 |
Data reduction software | AUTOMAR |
Phasing software | AMoRE |
Refinement software | CNS (1.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.090 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.042 | 0.270 |
Number of reflections | 8497 | |
<I/σ(I)> | 5.9 | 2.1 |
Completeness [%] | 95.3 | 95 |
Redundancy | 5.48 | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 293 | 0.1 M Tris ,0.1M Bicine, VAPOR DIFFUSION, HANGING DROP, temperature 293K |