1GMI

Structure of the c2 domain from novel protein kinase C epsilon

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Collection date	1999-08-15
Spacegroup name	P 21 21 21
Unit cell lengths	40.300, 56.500, 60.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.700
R-factor	0.234
Rwork	0.234
R-free	0.26200
Structure solution method	MIR
RMSD bond length	0.005
RMSD bond angle	1.400
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	CCP4
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	1.700	1.700
Rmerge	0.060	0.245 *
Number of reflections	15661 *
<I/σ(I)>	23.1	2.5
Completeness [%]	98.0	100 *
Redundancy	1.8	1.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *	20 *	16% PEG8000, 0.1M HEPES PH=7.5, 0.2M MGCL2., pH 7.60

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8 (mg/ml)
2	1	drop	DCPS	2 (mg/ml)	or DCPA
3	1	reservoir	PEG8000	16 (%(w/v))
4	1	reservoir	HEPES	100 (mM)
5	1	reservoir		0.2 (M)