Literature DB >> 2647518

Crystal structure of thermitase from Thermoactinomyces vulgaris at 2.2 A resolution.

A V Teplyakov1, I P Kuranova, E H Harutyunyan, C Frömmel, W E Höhne.   

Abstract

The crystal structure of thermitase from Thermoactinomyces vulgaris has been determined by x-ray diffraction at 2.2 A resolution. The structure was solved by a combination of single isomorphous replacement and molecular replacement methods. The structure was refined to a conventional R factor of 0.24 using restrained least square procedures CORELS and PROLSQ. The tertiary structure of thermitase is similar to that of subtilsin BPN'. The greatest differences between these structures are related to the insertions and deletions in the sequence.

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Year:  1989        PMID: 2647518     DOI: 10.1016/0014-5793(89)81194-9

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  1 in total

1.  An extracellular halophilic protease SptA from a halophilic archaeon Natrinema sp. J7: gene cloning, expression and characterization.

Authors:  Wanliang Shi; Xiao-Feng Tang; Yuping Huang; Fei Gan; Bing Tang; Ping Shen
Journal:  Extremophiles       Date:  2006-07-29       Impact factor: 3.035

  1 in total

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