1RJG

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-06-25
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	46.837, 74.098, 85.240
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	56.800 * - 1.870 *
R-factor	0.18624
Rwork	0.181
R-free	0.26200 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PBD ENTRY 1RJD
RMSD bond length	0.005
RMSD bond angle	0.840 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	56.800	1.970
High resolution limit [Å]	1.870	1.870
Rmerge	0.090 *
Total number of observations	71628 *
Number of reflections	21568
Completeness [%]	83.2	85.2
Redundancy	3.3 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	293	24% PEG 4000, 0.2M magnesium chloride, 0.1M Tris-HCl, pH 8.5, 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	PEG4000	24 (%)
3	1	reservoir		0.2 (M)
4	1	reservoir	Tris-HCl	0.1 (M)	pH8.5