1O6Z

1.95 A resolution structure of (R207S,R292S) mutant of malate dehydrogenase from the halophilic archaeon Haloarcula marismortui (holo form)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-06-17
Detector	ADSC CCD
Spacegroup name	C 1 2 1
Unit cell lengths	126.640, 114.420, 124.870
Unit cell angles	90.00, 93.11, 90.00

Refinement procedure

Resolution	42.260 * - 1.950
R-factor	0.19365
Rwork	0.190
R-free	0.26300 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1GT2
RMSD bond length	0.038 *
RMSD bond angle	2.450 *
Data reduction software	XDS
Data scaling software	BIOMOL
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	42.260	2.020
High resolution limit [Å]	1.950	1.950
Rmerge	0.064	0.143
Total number of observations	335871 *
Number of reflections	100475	5703 *
<I/σ(I)>	12.86	4.03
Completeness [%]	77.8	43.9
Redundancy	3.34	2.12

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7.6	4 *	2 M NACL, 25 MM TRIS PH 7.6, 2.5 MM NADH, 50% MPD

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	HEPES	50 (mM)	pH7.6
2	1	drop		4 (M)
3	1	drop	protein	20 (mg/ml)
4	1	reservoir	MPD	62 (%(v/v))