1RJE

Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2002-02-14
Detector	ADSC QUANTUM 4
Wavelength(s)	0.93300
Spacegroup name	P 65
Unit cell lengths	110.747, 110.747, 165.613
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	24.000 * - 2.000
R-factor	0.16138
Rwork	0.159
R-free	0.21000 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.790
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.000	2.110
High resolution limit [Å]	2.000	2.000
Rmerge	0.120 *
Total number of observations	294159 *
Number of reflections	76511
Completeness [%]	98.8	92
Redundancy	3.8 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6 *	293	15% PEG 8000, 0.2M ammonium sulfate, 0.1M MES, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	3 (mg/ml)
2	1	reservoir	PEG8000	15 (%)
3	1	reservoir	potassium phosphate	0.1 (M)	or sodium phosphate, pH4.6