1OHE

Structure of cdc14b phosphatase with a peptide ligand

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF
Synchrotron site	ESRF
Temperature [K]	100
Detector technology	CCD
Collection date	2002-09-15
Detector	ADSC CCD
Spacegroup name	C 1 2 1
Unit cell lengths	114.760, 53.150, 64.170
Unit cell angles	90.00, 117.48, 90.00

Refinement procedure

Resolution	33.000 - 2.200
R-factor	0.207
Rwork	0.207
R-free	0.25400 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.013
RMSD bond angle	1.530 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.300
High resolution limit [Å]	2.200	2.200
Rmerge	0.073 *	0.240 *
Total number of observations	62805 *
Number of reflections	17049 *
<I/σ(I)>	7.1	2.9
Completeness [%]	97.2	92.2
Redundancy	3.7	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	20 *	30% PEG 8000, 0.1 M ZINC ACETATE PH 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)