2TPT

STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	298
Detector technology	AREA DETECTOR
Collection date	1990-01
Detector	SIEMENS
Spacegroup name	P 43 21 2
Unit cell lengths	132.000, 132.000, 67.200
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.600
R-factor	0.207
Rwork	0.207
R-free	0.24400
Structure solution method	MULTIPLE ISOMORPHOUS REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	21.800 *
Data reduction software	XENGEN
Data scaling software	XENGEN
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	66.000	2.670
High resolution limit [Å]	2.600	2.580
Rmerge	0.077 *
Total number of observations	93897 *
Number of reflections	18521
Completeness [%]	95.7 *	86.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.5		Cook, W.J.,(1987) J. Biol. Chem., 262, 3788. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	52 (mg/ml)
2	1	drop	ammonium sulfate	35 (%)
3	1	drop	citrate	0.05 (M)
4	1	reservoir	ammonium sulfate	35 (%)
5	1	reservoir	citrate	0.05 (M)