2X0I

2.9 A RESOLUTION STRUCTURE OF MALATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS IN COMPLEX WITH NADH

Replaces:  1OJS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Detector	ADSC CCD
Spacegroup name	P 41 21 2
Unit cell lengths	112.964, 112.964, 71.294
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	56.480 - 2.910
R-factor	0.1557
Rwork	0.152
R-free	0.21860
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2hlp
RMSD bond length	0.008
RMSD bond angle	1.461
Data reduction software	XDS
Data scaling software	BIOMOL
Phasing software	AMoRE
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	59.760	3.010
High resolution limit [Å]	2.910	2.910
Rmerge	0.050	0.100
Number of reflections	8949
<I/σ(I)>	26.9	9.7
Completeness [%]	83.6	45.4
Redundancy	8.7	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		4		INITIAL PROTEIN DROPLET: 16 MG/ML PROTEIN, 10 MM NADH, 20 M RESERVOIR: 1.6 M AMMONIUM SULPHATE, 20% (V/V) GLYCEROL, 80 M DROPLET: EQUAL VOLUMES OF INITIAL PROTEIN DROPLET AND RESERVOIR WERE MIXED., pH 4.0