1THY

REFINED STRUCTURES OF SUBSTRATE-BOUND AND PHOSPHATE-BOUND THYMIDYLATE SYNTHASE FROM LACTOBACILLUS CASEI

Experimental procedure

Spacegroup name	P 61 2 2
Unit cell lengths	78.800, 78.800, 230.200
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	7.000 * - 2.900
R-factor	0.155
RMSD bond length	0.013
RMSD bond angle	3.100
Refinement software	PROLSQ

Data quality characteristics

	Overall
Low resolution limit [Å]	5.100 *
High resolution limit [Å]	2.900 *
Rmerge	0.068 *
Number of reflections	9633 *
Completeness [%]	95.6 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.8 *		taken from Hardy, L.W. et al (1987). Science, 235, 448-455. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	thymidylate synthase	10 (mg/ml)
2	1	drop	potassium phosphate	20 (mM)
3	1	reservoir	potassium phosphate	20 (mM)
4	1	reservoir	ammonium sulfate	15-20 (mM)
5	1	reservoir	dUMP	5 (mM)	with or without