首页> Biochemical and Biophysical Research Communications> Atomic resolution crystal structure of VcLMWPTP-1 from Vibrio cholerae O395: Insights into a novel mode of dimerization in the low molecular weight protein tyrosine phosphatase family

Atomic resolution crystal structure of VcLMWPTP-1 from Vibrio cholerae O395: Insights into a novel mode of dimerization in the low molecular weight protein tyrosine phosphatase family

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第一作者： Nath,S.

作者： Nath,S. ^[1] ; Banerjee,R. ; Sen,U.

作者单位： Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF ^[1]

关键词 Active dimer Bacterial protein phosphatases Low molecular weight protein tyrosine phosphatases X-ray crystallography

发布时间 2014-12-11

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Biochemical and Biophysical Research Communications

2014年450卷1期

390-395页

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Biochemical and Biophysical Research Communications

2014年450卷1期

390-395页

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Atomic resolution crystal structure of VcLMWPTP-1 from Vibrio cholerae O395: Insights into a novel mode of dimerization in the low molecular weight protein tyrosine phosphatase family

Biochemical and Biophysical Research Communications

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Atomic resolution crystal structure of VcLMWPTP-1 from Vibrio cholerae O395: Insights into a novel mode of dimerization in the low molecular weight protein tyrosine phosphatase family

Biochemical and Biophysical Research Communications

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Biochemical and Biophysical Research Communications

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