1BMD

DETERMINANTS OF PROTEIN THERMOSTABILITY OBSERVED IN THE 1.9 ANGSTROMS CRYSTAL STRUCTURE OF MALATE DEHYDROGENASE FROM THE THERMOPHILIC BACTERIUM THERMUS FLAVUS

Experimental procedure

Spacegroup name	P 21 21 21
Unit cell lengths	71.510, 87.590, 118.980
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	? - 1.900
R-factor	0.154
Rwork	0.154
RMSD bond length	0.016
RMSD bond angle	2.850
Phasing software	X-PLOR
Refinement software	TNT

Data quality characteristics

	Overall
High resolution limit [Å]	1.900 *
Rmerge	0.071 *
Total number of observations	376446 *
Number of reflections	63904 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	8.5 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	protein	13-15 (mg/ml)
2	1	reservoir	Tris	0.1 (M)
3	1	reservoir	PEG3350	20-24 (%)
4	1	reservoir		200-800 (mM)
5	1	reservoir	oxaloacetate	20 (mM)
6	1	reservoir	NADH	0.2-0.5 (mM)