3NEP

1.55A resolution structure of malate dehydrogenase from Salinibacter ruber

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2007-09-05
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9797
Spacegroup name	I 2 2 2
Unit cell lengths	76.110, 87.720, 100.450
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.036 - 1.551
R-factor	0.1691
Rwork	0.168
R-free	0.19170
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1guz
RMSD bond length	0.013
RMSD bond angle	1.333
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 1.6_288))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.900	1.600
High resolution limit [Å]	1.550	1.550
Rmerge	0.083	0.499
Number of reflections	47819
<I/σ(I)>	11.39	2.23
Completeness [%]	97.7	93.2
Redundancy	6.36	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4	298	1M LiCl, 0.1M Citric Acid, 10% PEG 6000, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
1	VAPOR DIFFUSION, HANGING DROP	4	298	1M LiCl, 0.1M Citric Acid, 10% PEG 6000, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
1	VAPOR DIFFUSION, HANGING DROP	4	298	1M LiCl, 0.1M Citric Acid, 10% PEG 6000, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K