1K1F

Structure of the Bcr-Abl Oncoprotein Oligomerization domain

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Detector technology	CCD
Collection date	2001-03-07
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9686,0.9789,0.9793
Spacegroup name	P 1 21 1
Unit cell lengths	35.988, 121.173, 60.432
Unit cell angles	90.00, 93.03, 90.00

Refinement procedure

Resolution	10.000 - 2.200
R-factor	0.262
Rwork	0.262
R-free	0.29500
Structure solution method	MAD
RMSD bond length	0.008 *
RMSD bond angle	1.420 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.200
Number of reflections	51251
Completeness [%]	99.0

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	6.5 *	293	ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	Vapor diffusion *	6.5 *	293	ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Bcr1-72C38A	10 (mg/ml)
2	1	reservoir	ammonium sulfate	2.5 (M)
3	1	drop	phosphate	20 (mM)
4	1	drop	guanidine hydrochloride	6 (M)	pH6.5