1OC2

The structure of NADH in the dTDP-D-glucose dehydratase (RmlB) enzyme

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	120
Detector technology	CCD
Collection date	2001-11-15
Detector	ADSC CCD
Spacegroup name	P 21 21 21
Unit cell lengths	61.410, 94.829, 183.543
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	34.700 * - 1.500
R-factor	0.173
Rwork	0.170
R-free	0.19900 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1kep
RMSD bond length	0.019
RMSD bond angle	0.008 *
Data reduction software	MOSFLM
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.700 *	1.530
High resolution limit [Å]	1.500	1.100
Rmerge	0.116	0.660
Total number of observations	2567266 *
Number of reflections	168795 *
<I/σ(I)>	4.3	1.2
Completeness [%]	98.6	98.6
Redundancy	3.5	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	5.4		used microseeding, Allard, S.T., (2002) Structure, 10, 81. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	3.6 (mg/ml)
2	1	drop	dithiothreitol	2.5 (mM)
3	1	drop	NAD+	4 (mM)
4	1	drop	dTDP-xylose	7 (mM)
5	1	reservoir	PEG4000	35 (%(w/v))
6	1	reservoir	citric acid	0.1 (M)	pH5.4
7	1	reservoir	ammonium sulfate	0.3 (M)