1E26

Design, Synthesis and X-ray Crystal Structure of a Potent Dual Inhibitor of Thymidylate Synthase and Dihydrofolate Reductase as an Antitumor Agent.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200HB
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1999-01-15
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 1 21 1
Unit cell lengths	37.332, 43.231, 61.241
Unit cell angles	90.00, 94.59, 90.00

Refinement procedure

Resolution	50.000 * - 2.000
R-factor	0.223 *
Rwork	0.218
R-free	0.29700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2cd2
RMSD bond length	0.008
RMSD bond angle	1.500
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000 *
High resolution limit [Å]	2.000	2.000 *
Rmerge	0.049 *
Number of reflections	11919
Completeness [%]	99.4	99.4 *
Redundancy	2.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	6	4 *	PROTEIN SOLUTION: WASHED AND CONCENTRATED 4 TUBES PCDHFR USING A CENTRICON 10 50 MM MES, 100MM KCL, B-NADPH, PH 6.0, A280/340 RATIO OF 24. WASHED WITH 50MM MES, 100MM KCL, PH 6.0, WASHED WITH 50MM MES, 100MM KCL, PH 6.0 TO A CONCENTRATION OF 6.5 MG/ML. RESERVOIR SOLUTION: 50% PEG2000MME, 50MM MES, 100MM, PH 6.0 SET UP MICROBATCH POLYTHERMAL GRADIENT EXPERIMENTS IN MICROPETS. DROPS WERE COMPOSED OF: 2.5 MICROLITERS PROTEIN SOLUTION 2.0 MICROLITERS PROTEIN SOLUTION 0.5 MICROLITERS 50MM MES, 100MM KCL, PH 6.0. MICROPETS WERE LEFT TO EQUILIBRATE ON THE POLYTHERMAL GRADIENT.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	9.8 (mg/ml)
2	1	1	PEG2000	50 (%(w/v))
3	1	1	MES	50 (mM)