3IMJ
Crystal Structure of the Grb2 SH2 Domain in Complex with a Cyclopropyl-constrained Ac-pTyr-Ile-Asn-NH2 Tripeptide Mimic
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-10-01 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 31.595, 85.511, 41.641 |
Unit cell angles | 90.00, 98.47, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.020 |
Rwork | 0.200 |
R-free | 0.22900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2huw |
RMSD bond length | 0.012 |
RMSD bond angle | 1.646 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.090 |
High resolution limit [Å] | 2.020 | 2.020 |
Rmerge | 0.047 | 0.265 |
Number of reflections | 13832 | |
<I/σ(I)> | 16.7 | |
Completeness [%] | 96.5 | 84.7 |
Redundancy | 2.1 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | Ligand in lyophilized powder form was dissolved in a 11.2 mg/mL solution of Grb2 SH2 in water such to give a protein/ligand molar ratio of 2:1. 4 uL of this solution was mixed with 3 uL of 0.2 M ammonium acetate, 0.1 M sodium acetate, 30% v/v PEG MW4000, pH 4.6 to create the hanging drop, which yielded crystals of the protein-ligand complex in the presence of the above-mentioned solution after four weeks at room temperature., VAPOR DIFFUSION, HANGING DROP, temperature 298K |