Literature DB >> 8107118

Crystallization and preliminary X-ray analysis of protocatechuate 3,4-dioxygenase from Acinetobacter calcoaceticus.

M W Vetting1, C A Earhart, D H Ohlendorf.   

Abstract

X-ray quality single crystals of protocatechuate 3,4-dioxygenase from Acinetobacter calcoaceticus were obtained by the hanging drop method. The intradiol dioxygenase crystallizes in the cubic space group I23 with unit cell dimensions a = b = c = 145.5 A. The dodecahedral crystals diffract to beyond 2.5 A resolution. The asymmetric unit contains one twelfth of the enzyme (alpha beta Fe+3)12 complex.

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Year:  1994        PMID： 8107118     DOI： 10.1006/jmbi.1994.1142

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


  3 in total

1.  Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases.

Authors:  D A D'Argenio; M W Vetting; D H Ohlendorf; L N Ornston
Journal:  J Bacteriol       Date:  1999-10       Impact factor: 3.490

2.  Combining localized PCR mutagenesis and natural transformation in direct genetic analysis of a transcriptional regulator gene, pobR.

Authors:  R G Kok; D A D'Argenio; L N Ornston
Journal:  J Bacteriol       Date:  1997-07       Impact factor: 3.490

3.  Spontaneous mutations in pcaH and -G, structural genes for protocatechuate 3,4-dioxygenase in Acinetobacter calcoaceticus.

Authors:  U Gerischer; L N Ornston
Journal:  J Bacteriol       Date:  1995-03       Impact factor: 3.490
  3 in total

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