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Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL41XU
Synchrotron site	SPring-8
Beamline	BL41XU
Temperature [K]	100
Detector technology	CCD
Collection date	2001-09-21
Detector	MARRESEARCH
Wavelength(s)	0.9791, 0.9793, 0.9000
Spacegroup name	P 61 2 2
Unit cell lengths	77.687, 77.687, 236.629
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 * - 2.300
Rwork	0.224
R-free	0.24900
Structure solution method	MAD
RMSD bond length	0.006
RMSD bond angle	24.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.330
High resolution limit [Å]	2.250	2.250
Rmerge	0.073 *	0.148 *
Total number of observations	383738 *
Number of reflections	20471 *
Completeness [%]	97.6	76.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	293	Shimomura, Y., (2002) Acta Crystallogr.,Sect.D, 58, 1365. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8.4 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)	pH8.0
3	1	drop		150 (mM)
4	1	drop	dithiothreitol	1 (mM)