6WO2

Crystal Structure of the Grb2 SH2 Domain in Complex with a Tripeptide: Ac-pY-Ac6c-N-isohexyl

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2011-06-30
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	32.225, 62.720, 90.137
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	51.480 - 2.000
R-factor	0.2039
Rwork	0.200
R-free	0.27540
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4p9v
RMSD bond length	0.020
RMSD bond angle	1.887
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	51.480	51.480	1.840
High resolution limit [Å]	1.780	3.830	1.780
Rmerge	0.072	0.042	0.544
Number of reflections	17182	1952	1414
<I/σ(I)>	14.1
Completeness [%]	94.6	98.7	79.9
Redundancy	5.6	5.6	3.2

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, ca. 10 mg/mL, was prepared. 4.0 ul of this solution was mixed with 3.0 ul of a precipitant solution containing 0.2 M sodium citrate tribasic dihydrate, 0.1 M HEPES, and 20% v/v 2-propanol (Hampton crystal screen I, condition no. 27), and allowed to equilibrate with 350 ul of the aforementioned precipitant well solution. Usable crystals grew after 4 weeks