1GV0

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	114.320, 149.420, 97.730
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.900 - 2.500
R-factor	0.221
Rwork	0.221
R-free	0.27500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	MDH WITH PDB-CODE 1GUZ
RMSD bond length	0.007
RMSD bond angle	1.150 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	EPMR
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.800	2.640
High resolution limit [Å]	2.500	2.500
Rmerge	0.070	0.254
Total number of observations	117908 *
Number of reflections	28459
Completeness [%]	100.0	100
Redundancy	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.4 *	15 *	20MG/ML,50MMTRIS-HCL,PH7.4,55%MPD, 100MMHEPES,PH7.5., pH 7.50

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	MPD	53 (%(v/v))
4	1	reservoir	HEPES	100 (mM)	pH7.5