1JG2

Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with adenosine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X8C
Synchrotron site	NSLS
Beamline	X8C
Temperature [K]	118
Detector technology	CCD
Collection date	2000-10-10
Detector	ADSC QUANTUM 4
Wavelength(s)	1.1000
Spacegroup name	P 21 21 21
Unit cell lengths	38.201, 52.522, 96.129
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	500.000 - 1.500
R-factor	0.221 *
Rwork	0.221
R-free	0.23600
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	1.400
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	500.000	1.550
High resolution limit [Å]	1.500	1.500
Rmerge	0.073	0.458
Total number of observations	119506 *
Number of reflections	30345
Completeness [%]	95.3	97.8 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	24 *	25% PEG 2000, 15% Glycerol, 0.2 M Ammonium Acetate pH 4.5, VAPOR DIFFUSION, HANGING DROP at 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	drop		0.5 (M)
3	1	drop	HEPES	20 (mM)
4	1	reservoir	PEG2000	25 (%(w/v))
5	1	reservoir	glycerol	15 (%(v/v))
6	1	reservoir	sodium acetate	0.2 (M)