Cloning, overexpression, purification and crystallization of malate dehydrogenase fromThermus thermophilus-Reference-Cited by-同舟云学术

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Cloning, overexpression, purification and crystallization of malate dehydrogenase fromThermus thermophilus

Published:2013-10-30 Issue:11 Volume:69 Page:1249-1251
ISSN:1744-3091
Container-title:Acta Crystallographica Section F Structural Biology and Crystallization Communications
language:
Short-container-title:Acta Cryst Sect F

Author:

Chang Yu-Yung,Hung Chih-Hung,Hwang Tzann-Shun,Hsu Chun-Hua

Publisher

International Union of Crystallography (IUCr)

Subject

Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics

Link

http://journals.iucr.org/f/issues/2013/11/00/ft5036/ft5036.pdf

Reference12 articles.

1. Measurement errors and their consequences in protein crystallography

2. Calculation of protein extinction coefficients from amino acid sequence data

3. Determinants of protein thermostability observed in the 1.9-.ANG. crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus

4. Application of Microbial Enzymes in Diagnostic Analysis

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2. The Genus Thermus: A Brief History of Cosmopolitan Extreme Thermophiles: Diversity, Distribution, Biotechnological Potential and Applications;Microorganisms for Sustainability;2021

3. Transcriptomic analysis of Pseudostellariae Radix from different fields using RNA-seq;Gene;2016-08

4. Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase;Journal of Zhejiang University-SCIENCE B;2016-04

5. Interface Matters: The Stiffness Route to Stability of a Thermophilic Tetrameric Malate Dehydrogenase;PLoS ONE;2014-12-01

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