3JDW

CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	290
Detector technology	IMAGE PLATE
Collection date	1995-11-11
Detector	MARRESEARCH
Spacegroup name	P 43 21 2
Unit cell lengths	83.760, 83.760, 199.650
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.400
R-factor	0.181
Rwork	0.181
Structure solution method	ISOMORPHOUS WITH PDB ENTRY 1JDW
Starting model (for MR)	1jdw
RMSD bond length	0.011
RMSD bond angle	25.110 *
Data reduction software	MOSFLM (V. 5.23)
Data scaling software	CCP4 ((AGROVATA)
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	8.000	2.430
High resolution limit [Å]	2.400	2.400
Rmerge	0.074	0.287
Number of reflections	25838
Completeness [%]	93.1	51.9
Redundancy	3.78	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7	22 *	1 PART OF AT38H (13-16 MG/ML) 2 PARTS OF PRECIPITANT (3% PEG 6000, 40 MM HEPES, 1MM GLUTATHIONE, PH7.0), SEVERAL DAYS AT ROOM TEMPERATURE, MACRO SEEDING.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	13-15 (mg/ml)
2	1	reservoir	PEG6000	3 (%)
3	1	reservoir	HEPES	40 (mM)
4	1	reservoir	beta-ME	2 (mM)