1AZY

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	NICOLET
Spacegroup name	P 1 21 1
Unit cell lengths	52.000, 78.000, 116.500
Unit cell angles	90.00, 91.50, 90.00

Refinement procedure

Resolution	8.000 - 3.000
R-factor	0.213 *
Rwork	0.204
R-free	0.27100 *
Structure solution method	MIR
RMSD bond length	0.009
RMSD bond angle	1.300 *
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]	30.700	2.890
High resolution limit [Å]	2.800	2.790
Rmerge	0.101 *
Total number of observations	81699 *
Number of reflections	22922
Completeness [%]	95.7	72.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.6		pH 4.6

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)