Crystallization and preliminary X-ray diffraction studies ofD-threo-3-hydroxyaspartate dehydratase isolated fromDelftiasp. HT23-Reference-Cited by-同舟云学术

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Crystallization and preliminary X-ray diffraction studies ofD-threo-3-hydroxyaspartate dehydratase isolated fromDelftiasp. HT23

Published:2013-09-28 Issue:10 Volume:69 Page:1131-1134
ISSN:1744-3091
Container-title:Acta Crystallographica Section F Structural Biology and Crystallization Communications
language:
Short-container-title:Acta Cryst Sect F

Author:

Matsumoto Yu,Yasutake Yoshiaki,Takeda Yuki,Tamura Tomohiro,Yokota Atsushi,Wada Masaru

Publisher

International Union of Crystallography (IUCr)

Subject

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

Link

http://journals.iucr.org/f/issues/2013/10/00/no5025/no5025.pdf

Reference22 articles.

1. Stereospecificity of the inhibition of l-glutamate and l-aspartate high affinity uptake in rat brain slices by threo-3-hydroxyaspartate

2. iMOSFLM: a new graphical interface for diffraction-image processing withMOSFLM

3. Novel approach to phasing proteins: derivatization by short cryo-soaking with halides

4. Pyridoxal Phosphate Enzymes: Mechanistic, Structural, and Evolutionary Considerations

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Structural insights into the substrate stereospecificity of d-threo-3-hydroxyaspartate dehydratase from Delftia sp. HT23: a useful enzyme for the synthesis of optically pure l-threo- and d-erythro-3-hydroxyaspartate;Applied Microbiology and Biotechnology;2015-02-26

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