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The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 32 2 1
Unit cell lengths	106.800, 106.800, 224.400
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 * - 2.800
Rwork	0.239
R-free	0.27500
Structure solution method	SAS with averaging
RMSD bond length	0.007
RMSD bond angle	22.800 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.830
High resolution limit [Å]	2.800	2.800
Rmerge	0.107	0.468
Number of reflections	36560
<I/σ(I)>	8.5	2.9
Completeness [%]	97.8 *	99.1 *
Redundancy	4.2	4.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	298	Magnesium formate, ethylene glycol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7 (mg/ml)
2	1	reservoir	magnesium formate	200 (mM)
3	1	reservoir	ethylene glycol	10 (%)