1OHC

Structure of the proline directed phosphatase cdc14

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF
Synchrotron site	ESRF
Temperature [K]	100
Detector technology	CCD
Collection date	2002-02-15
Detector	ADSC CCD
Spacegroup name	C 1 2 1
Unit cell lengths	114.702, 51.937, 65.070
Unit cell angles	90.00, 118.34, 90.00

Refinement procedure

Resolution	40.510 - 2.500
R-factor	0.201
Rwork	0.201
R-free	0.28200 *
Structure solution method	SIRAS
RMSD bond length	0.011 *
RMSD bond angle	1.550 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.600
High resolution limit [Å]	2.500	2.500
Rmerge	0.106	0.345
Total number of observations	38931 *
Number of reflections	11713
<I/σ(I)>	6.2
Completeness [%]	99.2 *	97.1
Redundancy	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	20 *	0.1 M TRIS ACETATE, 30% PEG 8000PH 8.0, 20 OC HANGING DROP VAPOUR DIFFUSION

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	reservoir	Tris-acetate	100 (mM)	pH8.0
3	1	reservoir	PEG4000	30 (%)
4	1	reservoir		0.2 (M)
5	1	reservoir	dithiothreitol	7 (mM)