1O27

Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima with FAD and BrdUMP at 2.3 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-1
Synchrotron site	SSRL
Beamline	BL9-1
Temperature [K]	100
Detector technology	CCD
Collection date	2002-03-20
Detector	ADSC QUANTUM 4r
Spacegroup name	P 21 21 21
Unit cell lengths	54.349, 116.428, 140.557
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.300
Rwork	0.188
R-free	0.23000
Structure solution method	MR
Starting model (for MR)	1kq4
RMSD bond length	0.007
RMSD bond angle	1.220
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SOLVE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.600 *	2.360
High resolution limit [Å]	2.300	2.300
Rmerge	0.081 *	0.445 *
Total number of observations	226323 *
Number of reflections	39615
<I/σ(I)>	17.5	3.5
Completeness [%]	98.0	93.1
Redundancy	5.7	5.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7.5	295	Kuhn, P., (2002) Proteins, 49, 142. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	Tris-HCl	100 (mM)	pH8.0
2	1	reservoir	PEG200	49 (%(w/v))	or 100mM HEPES, pH7.5
3	1	reservoir	PEG200	44 (%)