1ODJ

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	132.757, 132.757, 172.060
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	14.930 - 2.400
R-factor	0.221
Rwork	0.221
R-free	0.28600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	THE REFINED STRUCTURE OF PURINE NUCLEOSIDE PEPTIDASE FROM THERMUS THERMOPHILUS WAS USED AS STARTING MODEL FOR REFINEMENT
RMSD bond length	0.007
RMSD bond angle	1.400
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]	15.000	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.118	0.332
Number of reflections	58580
<I/σ(I)>	16.9	3.9
Completeness [%]	96.9	92.7
Redundancy	4.99

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH	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 LIGAND BOUND CRYSTALS WERE OBTAINED BY 7 H SOAKING OF NATIVE CRYSTALS IN SOLUTION CONTAINING 1.2M SODIUM ACETATE PH 6.3, 20MM AMMONIUM SULFATE, 2MM MAGNESIUM SULFATE AND 5MM GUANOSINE