6WM1

Crystal structure of the Grb2 SH2 domain in complex with a tripeptide: Ac-pY-Ac6c-N-phenylpropyl

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2011-05-18
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	36.010, 62.977, 90.889
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	51.760 - 1.800
R-factor	0.1802
Rwork	0.177
R-free	0.24480
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4p9v
RMSD bond length	0.023
RMSD bond angle	2.019
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER (2.1.4)
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	51.760	10.000	1.860
High resolution limit [Å]	1.800	3.880	1.800
Rmerge	0.040	0.032	0.113
Number of reflections	16789	2085	1770
<I/σ(I)>	46.7
Completeness [%]	84.6	97	92.4
Redundancy	10.2	9.5	10.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	An aqueous solution containing a 1.5 molar ratio of ligand to protein, 10 mg/mL, was prepared. 4.0 ul of this solution was mixed with 3.0 ul precipitant solution containing 0.1 M HEPES, pH 7.5, and 25% w/v polyethylene glycol, MW 10,000, and allowed to equilibrate with 350 ul of the aforementioned precipitant well solution at 298 K. Useable crystals grew after 4 weeks