1GY3

pCDK2/cyclin A in complex with MgADP, nitrate and peptide substrate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	150.710, 164.100, 72.430
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.700
R-factor	0.25 *
Rwork	0.250
R-free	0.31300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qmz
RMSD bond length	0.020 *
RMSD bond angle	2.000 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.810
High resolution limit [Å]	2.700	2.700
Rmerge	0.143	0.487
Total number of observations	319218 *
Number of reflections	45572
<I/σ(I)>	4.2	1.5
Completeness [%]	84.4	40.7
Redundancy	7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7	4 *	CRYSTALS WERE GROWN BY VAPOUR DIFFUSION AT 4C FROM SOLUTIONS CONTAINING 10 MG/ML PCDK2/CYCLIN A, 100 MM HEPES PH7.0, 2 MM SUBSTRATE PEPTIDE, 1MM ADP, 1.0 M LI2SO4. CRYSTALS WERE TRANSFERRED TO 20%PEG 8K, 100 MM HEPES PH 7.0, 10 MM SUBSSTRATE PEPTIDE, 5 MM MG(NO3)2

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	pCDK2/cyclinA	10 (mg/ml)
2	1	drop	HEPES	100 (mM)	pH7.0
3	1	drop	peptide	2 (mM)
4	1	drop	ADP	1 (mM)
5	1	drop		1.05-1.15 (M)