1.95 A resolution structure of (R207S,R292S) mutant of malate dehydrogenase from the halophilic archaeon Haloarcula marismortui (holo form)

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

Insights Into the Molecular Relationships between Malate and Lactate Dehydrogenases: Structural and Biochemical Properties of Monomeric and Dimeric Intermediates of a Mutant of Tetrameric L-[Ldh-Like] Malate Dehydrogenase from the Halophilic Archaeon Haloarcula Marismortui

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

Mutation at a Single Acidic Amino Acid Enhances the Halophilic Behaviour of Malate Dehydrogenase from Haloarcula Marismortui in Physiological Salts

Cloning, Sequencing, and Expression in Escherichia Coli of the Gene Coding for Malate Dehydrogenase of the Extremely Halophilic Archaebacterium Haloarcula Marismortui

2 M NACL, 25 MM TRIS PH 7.6, 2.5 MM NADH, 50% MPD

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)

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

ENGINEERED MUTATION ARG 188 SER AND ARG 267 SER IN CHAINS A, B, C AND D

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE REGION 100-107 OF B AND D CHAIN IS DISORDERED. THE RESIDUES 101-106 IN THESE DISORDERED REGIONS COULD NOT BE MODELLED AND ARE OMITTED FROM THE MODEL.

HALOPHILIC, ION-BINDING, PROTEIN-SOLVENT INTERACTION, MALATE DEHYDROGENASE, OXIDOREDUCTASE