3KFJ

Crystal Structure of the Grb2 SH2 Domain in Complex with a Flexible Ac-pY-E-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	2007-04-21
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 43 21 2
Unit cell lengths	41.873, 41.873, 108.811
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.020
Rwork	0.198
R-free	0.22960
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3c7i
RMSD bond length	0.012
RMSD bond angle	1.622
Data reduction software	HKL-2000
Data scaling software	HKL-2000
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	0.050	0.102
Number of reflections	6814
<I/σ(I)>	63.8
Completeness [%]	98.4	100
Redundancy	8.8	9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	298	Ligand in lyophilized powder form was dissolved in a 9.5 mg/mL solution of Grb2 SH2 in water such to give a protein/ligand molar ratio of 2:1. 4uL of this solution was mixed with 3uL of 0.1 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