1RJD

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 BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2002-02-14
Detector	MARRESEARCH
Wavelength(s)	0.94, 0.9792, 0.9795, 0.9184
Spacegroup name	P 65
Unit cell lengths	110.683, 110.683, 165.879
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	52.000 * - 1.800
R-factor	0.17968
Rwork	0.178
R-free	0.21400 *
Structure solution method	MAD
RMSD bond length	0.005 *
RMSD bond angle	0.780 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	SOLVE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	52.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.130 *
Total number of observations	631127 *
Number of reflections	106254
Completeness [%]	100.0	100
Redundancy	5.9 *

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