1OPJ

Structural basis for the auto-inhibition of c-Abl tyrosine kinase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2002-07-10
Detector	ADSC QUANTUM 4
Wavelength(s)	0.934
Spacegroup name	P 1
Unit cell lengths	41.844, 63.507, 64.051
Unit cell angles	67.91, 79.76, 84.88

Refinement procedure

Resolution	30.000 * - 1.700 *
R-factor	0.21
Rwork	0.210
R-free	0.24200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1iep
RMSD bond length	0.008
RMSD bond angle	21.800 *
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.800
High resolution limit [Å]	1.700	1.700
Rmerge	0.090 *	0.509 *
Total number of observations	268488 *
Number of reflections	61592
<I/σ(I)>	9.41	2.84
Completeness [%]	92.9	75.8
Redundancy	4.4	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	4 *	22% PEG 4000, 100 mM MES pH 5.6, 200 mM magnesium chloride, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	22 (%(w/v))
2	1	reservoir	MES	100 (mM)	pH5.6
3	1	reservoir		200 (mM)
4	1	drop	Tris-HCl	20 (mM)	pH8.0
5	1	drop		100 (mM)
6	1	drop	dithiothreitol	5 (mM)
7	1	drop	protein	35 (mg/ml)