2BZG

Crystal structure of thiopurine S-methyltransferase.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2005-07-14
Detector	ADSC CCD
Spacegroup name	P 42 21 2
Unit cell lengths	85.486, 85.486, 69.362
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	60.410 - 1.580
R-factor	0.214
Rwork	0.213
R-free	0.24900
Structure solution method	SAD
RMSD bond length	0.020
RMSD bond angle	1.384
Data reduction software	d*TREK
Data scaling software	d*TREK
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.390	1.640
High resolution limit [Å]	1.580	1.580
Rmerge	0.070	0.270
Number of reflections	67746
<I/σ(I)>	11.8	4.1
Completeness [%]	99.0	92.9
Redundancy	7.09	4.24

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	PROTEIN WAS CRYSTALLIZED IN THE PRESENCE OF 6-MERCAPTOPURINE-9-B, D-RIBOFURANOSIDE (PROTEIN: 6-MP-RIBOFURANOSIDE= 1:10) USING THE HANGING DROP VAPOR DIFFUSION METHOD AT 20C BY MIXING 1.5 UL OF THE PROTEIN SOLUTION WITH 1.5 UL OF THE RESERVOIR SOLUTION CONTAINING 24% PEG3350, 0.2 M KCNS, 0.1 M BISTRIS PROPANE, PH 7.0.