Expression, purification, crystallization, and preliminary X-ray analysis of the N-terminal domain of Escherichia coli adenylyl transferase

Yibin Xu*, Daying Wen, Paula Clancy, Paul D. Carr, David L. Ollis, Subhash G. Vasudevan

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    6 Citations (Scopus)

    Abstract

    A soluble N-terminal domain of the Escherichia coli adenylyl transferase (ATase) is responsible for deadenylylation activity of the intact enzyme. Previous studies of the deadenylylation activity have involved a fragment, AT-N423 (residues 1 to 423), which was extended by 17 amino acids to give AT-N440. This new domain is truncated at the end of a predicted helix and prior to a Q-linker. The domain was found to be very soluble and stable so that it could be purified to homogeneity and crystallized. This construct has deadenylylation activity that is independent of the low nitrogen status indicator PII-UMP. The crystals belong to space group P3121 or its enantiomorph P3221 with a = b = 116.6 Å and c = 67.6 Å.

    Original languageEnglish
    Pages (from-to)142-146
    Number of pages5
    JournalProtein Expression and Purification
    Volume34
    Issue number1
    DOIs
    Publication statusPublished - Mar 2004

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