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pubmed-article:11053848pubmed:abstractTextThe lethal factor (LF) produced by Bacillus anthracis is a Zn(2+)-dependent endopeptidase which specifically cleaves the N-terminal tail of several MAP kinase kinases (MAPKKs). The recombinant expression, purification and crystallization of LF and of an inactive mutant consisting of a single amino-acid substitution in the conserved catalytic site are reported here. Both proteins crystallize in the cubic space group I432.lld:pubmed
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pubmed-article:11053848pubmed:authorpubmed-author:VitaliCClld:pubmed
pubmed-article:11053848pubmed:authorpubmed-author:BernardiLLlld:pubmed
pubmed-article:11053848pubmed:authorpubmed-author:MontecuccoCClld:pubmed
pubmed-article:11053848pubmed:authorpubmed-author:MusacchioAAlld:pubmed
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pubmed-article:11053848pubmed:pagination1449-51lld:pubmed
pubmed-article:11053848pubmed:dateRevised2007-7-24lld:pubmed
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pubmed-article:11053848pubmed:year2000lld:pubmed
pubmed-article:11053848pubmed:articleTitleExpression, crystallization and preliminary X-ray diffraction studies of recombinant Bacillus anthracis lethal factor.lld:pubmed
pubmed-article:11053848pubmed:affiliationCentro CNR Biomembrane and Dipartimento di Scienze Biomediche, Università di Padova, 35121 Padova, Italy.lld:pubmed
pubmed-article:11053848pubmed:publicationTypeJournal Articlelld:pubmed
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