1OTP

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

Experimental procedure

Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1990-01
Detector	RIGAKU RAXIS
Spacegroup name	I 2 2 2
Unit cell lengths	78.000, 97.400, 137.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.800
R-factor	0.201
Rwork	0.201
R-free	0.24800
Structure solution method	SINGLE ISOMORPHOUS REPLACEMENT
RMSD bond length	0.009 *
RMSD bond angle	22.300 *
Data reduction software	XENGEN
Data scaling software	XENGEN
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	79.500	2.670
High resolution limit [Å]	2.600	2.580
Rmerge	0.071 *
Total number of observations	57343 *
Number of reflections	14713
Completeness [%]	87.3	65.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.6 *		PROTEIN WAS CRYSTALLIZED FROM 0.9 - 1.2 M SODIUM CITRATE (PH 6.4 - 6.8) AND 2MM DTT AT ROOM TEMPERATURE USING HANGING DROP METHOD

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	33 (mg/ml)
2	1	drop	PEG4000	7.5 (%)
3	1	drop	citrate	50 (mM)
4	1	reservoir	PEG4000	15 (%)
5	1	reservoir	sodium citrate	50 (mM)