Literature DB >> 3783675

Crystallization and preliminary X-ray diffraction study of an endoglucanase from Clostridium thermocellum.

G Joliff, P Béguin, J Millet, J P Aubert, P Alzari, M Juy, R J Poljak.   

Abstract

Endoglucanase D, a cellulose degradation enzyme from Clostridium thermocellum has been cloned in Escherichia coli, purified and crystallized. The crystals are trigonal, space group P3(1)12 (or P3(2)12) with a = 57.7 (+/- 0.1) A, c = 192.1 (+/- 0.2) A, and diffract X-rays to a resolution of 2.8 A. They are suitable for a high-resolution X-ray diffraction analysis.

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Year:  1986        PMID： 3783675     DOI： 10.1016/0022-2836(86)90396-7

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


  4 in total

1.  Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum.

Authors:  P Tomme; J van Beeumen; M Claeyssens
Journal:  Biochem J       Date:  1992-07-01       Impact factor: 3.857

2.  Nucleotide sequence of the cellulase gene celD encoding endoglucanase D of Clostridium thermocellum.

Authors:  G Joliff; P Béguin; J P Aubert
Journal:  Nucleic Acids Res       Date:  1986-11-11       Impact factor: 16.971

3.  The catalytic domain of endoglucanase A from Clostridium cellulolyticum: effects of arginine 79 and histidine 122 mutations on catalysis.

Authors:  A Belaich; H P Fierobe; D Baty; B Busetta; C Bagnara-Tardif; C Gaudin; J P Belaich
Journal:  J Bacteriol       Date:  1992-07       Impact factor: 3.490

4.  A CsgD-independent pathway for cellulose production and biofilm formation in Escherichia coli.

Authors:  Sandra Da Re; Jean-Marc Ghigo
Journal:  J Bacteriol       Date:  2006-04       Impact factor: 3.490
  4 in total

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