3IMD

Crystal Structure of the Grb2 SH2 Domain in Complex with a Flexible Ac-pY-Q-N-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	2007-03-01
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	42.239, 42.243, 110.384
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.000
Rwork	0.199
R-free	0.23700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3c7i
RMSD bond length	0.012
RMSD bond angle	1.544
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	1.850
High resolution limit [Å]	1.790	1.790
Rmerge	0.049	0.084
Number of reflections	18279
<I/σ(I)>	50.8
Completeness [%]	94.7	96.1
Redundancy	5.9	5.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	298	Ligand in lyphilized powder form was dissolved in a 9.1 mg/mL solution of Grb2 SH2 in water such to give a protein/ligand molar ratio of 2:1. 3 uL of this solution was mixed with 4 uL of 0.2 M MgCl2 x 6H2O, 30% w/v PEG MW4000, 0.1 M TRIS, pH 8.5 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