1P22

Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity on the SCFbeta-TrCP1 ubiquitin ligase

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	103
Detector technology	CCD
Collection date	2001-12-23
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9500
Spacegroup name	P 31
Unit cell lengths	82.600, 82.600, 111.500
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.950
R-factor	0.23315
Rwork	0.230
R-free	0.28600 *
Structure solution method	MAD
RMSD bond length	0.014 *
RMSD bond angle	1.855 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	DM
Refinement software	REFMAC (5.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.025
High resolution limit [Å]	2.950	2.950
Rmerge	0.040 *	0.430 *
Total number of observations	52111 *
Number of reflections	17628
Completeness [%]	99.3	99.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.8	298	PEG4000, sodium citrate, Bis-Tris Propane, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	beta-catenin peptide	5 (mg/ml)
3	1	reservoir	PEG4000	16-20 (%)
4	1	reservoir	sodium citrate	320 (mM)
5	1	reservoir	BTP	100 (mM)	pH6.8