1DL5

PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-06-11
Detector	RIGAKU RAXIS IV
Spacegroup name	P 1 21 1
Unit cell lengths	51.060, 98.910, 76.860
Unit cell angles	90.00, 105.66, 90.00

Refinement procedure

Resolution	15.000 - 1.800
R-factor	0.182
Rwork	0.182
R-free	0.20300
Structure solution method	MIR
RMSD bond length	0.006
RMSD bond angle	1.380 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.850
High resolution limit [Å]	1.650 *	1.800
Rmerge	0.053	0.237
Number of reflections	66308
<I/σ(I)>	18.3	10
Completeness [%]	97.6	95.7
Redundancy	7	7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.5	18 *	THREE MICROLITERS OF PROTEIN AT A CONCENTRATION OF 6.3MGS/ML IN 10MM TRIS PH 8.0, 200MM NACL, 5% GLYCEROL, LMM DTT, 5MM BME AND 0.1MM EDTA WERE MIXED WITH THREE MICROLITERS OF A RESERVOIR SOLUTION OF 28% PEG400, 100MM SODIUM ACETATE PH 4.5, AND 100MM CADMIUM CHLORIDE AND EQUILIBRATED AGAINST THE SAME., VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG400	28 (%(v/v))
2	1	reservoir		100 (mM)
3	1	reservoir		100 (mM )	or ZnSO4