1RJF

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)	0.98000
Spacegroup name	P 65
Unit cell lengths	112.395, 112.395, 162.848
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.250
R-factor	0.1857
Rwork	0.183
R-free	0.23900 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.800
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]	30.000	2.370
High resolution limit [Å]	2.250	2.250
Rmerge	0.070 *
Total number of observations	290033 *
Number of reflections	53908
Completeness [%]	97.6	86
Redundancy	5.4 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	293	15% PEG 8000, 0.1M K/NaPO4, pH 4.6, 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)