4AOI

Crystal structure of C-MET kinase domain in complex with 4-(3-((1H- pyrrolo(2,3-b)pyridin-3-yl)methyl)-(1,2,4)triazolo(4,3-b)(1,2,4) triazin-6-yl)benzonitrile

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	96
Detector technology	CCD
Collection date	2006-03-09
Detector	ADSC QUANTUM 210
Spacegroup name	P 21 21 2
Unit cell lengths	76.809, 93.758, 46.432
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.610 - 1.900
Rwork	0.173
R-free	0.21400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2wkm
RMSD bond length	0.004
RMSD bond angle	0.800
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CCP4
Refinement software	CNX (2005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.940
High resolution limit [Å]	1.900	1.900
Rmerge	0.060	0.300
Number of reflections	26935
<I/σ(I)>	22	3.9
Completeness [%]	99.3	98
Redundancy	3.6	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		286	CRYSTALS WERE OBTAINED AT 13 DEGREES CELCIUS FROM HANGING DROPS CONTAINING 1.2 MICROLITERS OF PROTEIN: COMPOUND SOLUTION (1:5 MOLAR RATIO) AND 1.2 MICROLITERS OF PRECIPITATING SOLUTION (0.05 M CITRATE-PHOSPHATE, PH 4.6, 0-25 MM NACL, 21 % (W/V) PEG-3350). TO OBTAIN LARGER CRYSTALS, STREAK SEEDING WAS EMPLOYED USING THE CRYSTALS JUST MENTIONED AS DONORS, UNDER THE SAME CONDITIONS EXCEPT 275 MM NACL WAS USED AND THE DROPS WERE EQUILIBRATED OVERNIGHT BEFORE SEEDING WAS PERFORMED.