Cloning, overexpression, purification and crystallization of malate dehydrogenase from Thermus thermophilus.
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Crystal structures and molecular dynamics simulations of thermophilic malate dehydrogenase reveal critical loop motion for co-substrate bindingCrystallization of the C-terminal redox domain of the sulfur-assimilatory enzyme APR1 from Arabidopsis thaliana.Interface matters: the stiffness route to stability of a thermophilic tetrameric malate dehydrogenase.Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase*.
P2860
Cloning, overexpression, purification and crystallization of malate dehydrogenase from Thermus thermophilus.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 30 October 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Cloning, overexpression, purif ...... ase from Thermus thermophilus.
@en
Cloning, overexpression, purif ...... ase from Thermus thermophilus.
@nl
type
label
Cloning, overexpression, purif ...... ase from Thermus thermophilus.
@en
Cloning, overexpression, purif ...... ase from Thermus thermophilus.
@nl
prefLabel
Cloning, overexpression, purif ...... ase from Thermus thermophilus.
@en
Cloning, overexpression, purif ...... ase from Thermus thermophilus.
@nl
P2093
P2860
P1476
Cloning, overexpression, purif ...... ase from Thermus thermophilus.
@en
P2093
Chih-Hung Hung
Tzann-Shun Hwang
Yu-Yung Chang
P2860
P304
P356
10.1107/S174430911302472X
P50
P577
2013-10-30T00:00:00Z