1ODL

PURINE NUCLEOSIDE PHOSPHORYLASE FROM THERMUS THERMOPHILUS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-D
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2003-01-15
Detector	RIGAKU IMAGE PLATE, RAXIS-VII
Spacegroup name	P 43 21 2
Unit cell lengths	132.002, 132.002, 170.145
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.990 - 2.100
R-factor	0.187
Rwork	0.187
R-free	0.23400
Structure solution method	OTHER
RMSD bond length	0.005
RMSD bond angle	22.900 *
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.100	0.331
Number of reflections	86945
<I/σ(I)>	15.2	5.05
Completeness [%]	98.7	97.7
Redundancy	6.59

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	microseeding *	6.3	291	MICROBATCH METHOD UNDER OIL WAS USED.15.1 MG/ML OF PROTEIN SOLUTION CONTAINING 0.02M DTT WAS MIXED WITH 1.65M SODIUM ACETATE AND 0.1M MES PH 6.3. THE CRYSTALLIZATION TEMPERATURE WAS 291 K. PARATONE-N OIL MIXED WITH 10% W/W OF GLYCEROL WAS USED FOR CRYOPROTECTION SULFATE ION BOUND CRYSTALS WERE OBTAINED BY 7 H SOAKING OF NATIVE CRYSTALS IN SOLUTION CONTAINING 1.2M SODIUM ACETATE PH 6.3 AND 20MM AMMONIUM SULFATE

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	dithiothreitol	0.02 (M)
3	1	reservoir	sodium acetate	1.65 (M)
4	1	reservoir	MES	0.1 (M)