1A81

CRYSTAL STRUCTURE OF THE TANDEM SH2 DOMAIN OF THE SYK KINASE BOUND TO A DUALLY TYROSINE-PHOSPHORYLATED ITAM

Experimental procedure

Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-04
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	85.500, 146.900, 91.500
Unit cell angles	90.00, 97.60, 90.00

Refinement procedure

Resolution	30.000 - 3.000
R-factor	0.226
Rwork	0.226
R-free	0.31700
Structure solution method	MULTIPLE ISOMORPHOUS REPLACEMENT
RMSD bond length	0.016
RMSD bond angle	1.900
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	X-PLOR (3.85)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	3.070
High resolution limit [Å]	3.000	3.000
Rmerge	0.051 *
Total number of observations	202021 *
Number of reflections	40670
Completeness [%]	89.8	74.1
Redundancy	5	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5		10% (W/V) PEG800, 10% (V/V) PEG 200, 0.1M TRIS HCL PH 8.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	17.5 (mg/ml)
2	1	drop	PEG8000	4.5-6 (%(w/v))
3	1	drop	PEG200	5 (%(v/v))
4	1	drop	Tris-HCl	0.05 (M)
5	1	reservoir	PEG8000	9-12 (%(w/v))
6	1	reservoir	PEG200	10 (%(v/v))
7	1	reservoir	Tris-HCl	0.1 (M)