1GV1

Structural Basis for Thermophilic Protein Stability: Structures of Thermophilic and Mesophilic Malate Dehydrogenases

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	64.425, 85.824, 117.498
Unit cell angles	90.00, 104.61, 90.00

Refinement procedure

Resolution	19.920 - 2.500
R-factor	0.216
Rwork	0.216
R-free	0.30500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	MDH WITH PDB-CODE 1GUZ
RMSD bond length	0.007
RMSD bond angle	1.260 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS (1.0)
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000 *	2.590
High resolution limit [Å]	2.500	2.500
Rmerge	0.079	0.251
Total number of observations	388140 *
Number of reflections	37824
<I/σ(I)>	11	2.5
Completeness [%]	92.5	84.1
Redundancy	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.4 *		~20 MG/ML, 50 MM TRIS-HCL, PH 7.4, 40 % PEG-MME5000, 100 MM

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	Tris-HCl	50 (mM)	pH7.4
3	1	reservoir	PEG5000 MME	40 (%)
4	1	reservoir	sodium succinate	100 (mM)	pH6.0