2.15 A resolution structure of the wild type malate dehydrogenase from Haloarcula marismortui after first radiation burn (radiation damage series)

Specific Radiation Damage to Acidic Residues and its Relation to Their Chemical and Structural Environment.

The Oligomeric States of Haloarcula Marismortui Malate Dehydrogenase are Modulated by Solvent Components as Shown by Crystallographic and Biochemical Studies

Halophilic Adaptation: Novel Solvent Protein Interactions Observed in the 2.9 And 2.6 A Resolution Structures of the Wild Type and a Mutant of Malate Dehydrogenase from Haloarcula Marismortui

Structural Features that Stabilize Halophilic Malate-Dehydrogenase from an Archaebacterium.

3UL OF PROTEIN PLUS 4UL OF MPD WERE EQUILIBRATED AGAINST 58% MPD VIA THE SITTING DROP REVERSE VAPOUR DIFFUSION TECHNIQUE, pH 7.00

CRYSTAL STRUCTURE OF THE WILD TYPE HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM

R207S,R292S MUTANT OF MALATE DEHYDROGENASE FROM THE HALOPHILIC ARCHAEON HALOARCULA MARISMORTUI (HOLO FORM)

MALATE DEHYDROGENASE (HALOPHILIC) COMPLEXED WITH NICOTINAMIDE ADENINE DINUCLEOTIDE (NAD)

1.95 A RESOLUTION STRUCTURE OF (R207S, R292S) MUTANT OF MALATE DEHYDROGENASE FROM THE HALOPHILIC ARCHAEON HALOARCULA MARISMORTUI (HOLO FORM)

CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM

2.25 A RESOLUTION STRUCTURE OF THE WILD TYPE MALATE DEHYDROGENASE FROM HALOARCULA MARISMORTUI AFTER SECOND RADIATION BURN ( RADIATION DAMAGE SERIES)

2.0 A RESOLUTION STRUCTURE OF THE WILD TYPE MALATE DEHYDROGENASE FROM HALOARCULA MARISMORTUI (RADIATION DAMAGE SERIES)

SIDE CHAINS ATOMS WITHOUT ELECTRON DENSITY APPEARING AT 1 SIGMA LEVEL IN 3MFO-2DFC MAPS WERE REMOVED FROM THE MODEL.RESIDUES IN POSITION 100-107 WERE EXCLUDED FROM THE MODEL OF MONOMERS B AND D BECAUSE DISORDERED.

NAD, HALOPHILE, OXIDOREDUCTASE, RADIATION DAMAGE, MALATE DEHYDROGENASE, TRICARBOXYLIC ACID CYCLE