1HW3

STRUCTURE OF HUMAN THYMIDYLATE SYNTHASE SUGGESTS ADVANTAGES OF CHEMOTHERAPY WITH NONCOMPETITIVE INHIBITORS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	120
Detector technology	CCD
Collection date	2000-08-25
Detector	SBC-1
Wavelength(s)	0.9793
Spacegroup name	P 31 2 1
Unit cell lengths	95.824, 95.824, 83.207
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	6.000 - 2.000
R-factor	0.203 *
Rwork	0.203
R-free	0.23000
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.300
Data reduction software	d*TREK
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.033	0.310
Total number of observations	144310 *
Number of reflections	28819
<I/σ(I)>	19.5
Completeness [%]	96.0	100
Redundancy	1.9	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.8	298	ammonium sulfate, tris buffer, potassium phosphate, 2-mercaptoethanol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	18 (mg/ml)
10	1	reservoir	Tris-HCl	100 (mM)
2	1	drop	EDTA	1 (mM)
3	1	drop	2-ME	10 (mM)
4	1	drop		0.1-1 (M)
5	1	drop	imidazole	100 (mM)
6	1	drop	Tris-HCl	50 (mM)
7	1	reservoir	ammonium sulfate	38-50 (%sat)
8	1	reservoir	potassium phosphate	40 (mM)
9	1	reservoir	2-ME	20 (mM)