1A25

C2 DOMAIN FROM PROTEIN KINASE C (BETA)

Experimental procedure

Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	133
Detector technology	CCD
Collection date	1996-10
Detector	PRINCETON 2K
Spacegroup name	P 43 21 2
Unit cell lengths	77.798, 77.798, 140.826
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.700
R-factor	0.222
Rwork	0.222
R-free	0.25400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rsy
RMSD bond length	0.010
RMSD bond angle	24.000 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.900
High resolution limit [Å]	2.700	2.700
Rmerge	0.136	0.130
Number of reflections	12297
<I/σ(I)>	13	8
Completeness [%]	98.5	95
Redundancy	8.9	5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.4 *	21 *	PROTEIN WAS CRYSTALLIZED FROM 15% PEG1500, 100 MM MES, PH 6.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	PEG1500	15 (%(w/v))
2	1	drop		2 (mM)
3	1	drop	o-phospho-L-serine	2 (mM)
4	1	drop	MES	100 (mM)