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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulatory domain of aspartokinase (Rv3709c) from Mycobacterium tuberculosis

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  • Linda Schuldt
  • ,
  • Ruth Suchowersky, EMBL Hamburg Outstation, Tyskland
  • Katharina Veith, EMBL Hamburg Outstation, Tyskland
  • Jochen Mueller-Dieckmann, EMBL Hamburg Outstation, Tyskland
  • Manfred S Weiss, EMBL Hamburg Outstation, Tyskland
The regulatory domain of Mycobacterium tuberculosis aspartokinase (Mtb-AK, Mtb-Ask, Rv3709c) has been cloned, heterologously expressed in Escherichia coli and purified using standard chromatographic techniques. Screening for initial crystallization conditions using the regulatory domain (AK-β) in the presence of the potential feedback inhibitor threonine identified four conditions which yielded crystals suitable for X-ray diffraction analysis. From these four conditions five different crystal forms of Mtb-AK-β resulted, three of which belonged to the orthorhombic system, one to the tetragonal system and one to the monoclinic system. The highest resolution (1.6 Å) was observed for a crystal form belonging to space group P2(1)2(1)2(1), with unit-cell parameters a=53.70, b=63.43, c=108.85 Å and two molecules per asymmetric unit.
OriginalsprogEngelsk
TidsskriftActa Crystallographica. Section F: Structural Biology and Crystallization Communications Online
Vol/bind67
NummerPart 3
Sider (fra-til)380-385
Antal sider6
ISSN2053-230X
DOI
StatusUdgivet - mar. 2011

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