3IN7

Crystal Structure of the Grb2 SH2 Domain in Complex with a Cyclopropyl-constrained 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	2007-05-25
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	40.384, 63.955, 92.725
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.000
Rwork	0.229
R-free	0.25000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2huw
RMSD bond length	0.012
RMSD bond angle	1.659
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	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.054	0.305
Number of reflections	19967
<I/σ(I)>	20.4
Completeness [%]	71.6	6.6
Redundancy	4.5	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	Ligand in lyophilized powder form was dissolved in a 7.6 mg/mL solution of Grb2 SH2 in water such to give a protein/ligand molar ratio of 1.7:1. 3.5 uL of this solution was mixed with 3.5 uL of 0.1 M HEPES, 20% w/v PEG MW10,000, pH 7.5 to create the hanging drop, which yielded crystals of the protein-ligand complex in the presence of the above-mentioned solution after two weeks at room temperature., VAPOR DIFFUSION, HANGING DROP, temperature 298K