1FFL

CRYSTAL STRUCTURE OF THE APO-THYMIDYLATE SYNTHASE R166Q MUTANT

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR571
Temperature [K]	298
Detector technology	DIFFRACTOMETER
Collection date	1997-05-04
Detector	ENRAF-NONIUS FAST
Spacegroup name	I 21 3
Unit cell lengths	132.500, 132.500, 132.500
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.130 - 2.940
R-factor	0.17 *
Rwork	0.171
R-free	0.21000 *
Structure solution method	Fourier Difference Maps
Starting model (for MR)	Wildtype Binary Complex of E.coli thymidylate synthase
RMSD bond length	0.008 *
RMSD bond angle	1.400 *
Data reduction software	MADNESS
Data scaling software	CCP4 ((AGROVATA)
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.000 *	3.020
High resolution limit [Å]	2.940	2.940
Rmerge	0.090	0.380
Number of reflections	8138
<I/σ(I)>	7.4
Completeness [%]	96.0 *	96
Redundancy	7	6.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	8 *	298	Montfort, W.R., (1990) Biochemistry, 29, 6964. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5-9 (mg/mL)
2	1	drop	potasssium	20 (mM)
3	1	drop	ammonium	2.3 (M)
4	1	drop	dUMP	100 (mM)
5	1	drop	CB3717	4.78 (mM)
6	1	reservoir	potassium	20 (mM)
7	1	reservoir	disodium ethylenediaminetetraacetic acid	0.1 (mM)
8	1	reservoir	beta-mercaptoethanol	20 (mM)