1GUZ

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7A
Temperature [K]	100
Spacegroup name	P 21 21 21
Unit cell lengths	83.890, 117.390, 125.330
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.580 - 2.000
R-factor	0.242 *
Rwork	0.243
R-free	0.29200
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	1.190 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.125	0.297
Total number of observations	502001 *
Number of reflections	82230
<I/σ(I)>	9	3
Completeness [%]	97.7	85.6
Redundancy	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5		0.15 M NAAC 75 MM TRIS HCL, PH 8.5, 22.5 % PEG 4000

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	sodium acetate	0.15 (M)
3	1	drop	Tris-HCl	75 (mM)	pH8.5
4	1	reservoir	PEG4000	22.5 (%)