Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapB (Rv2773c) from Mycobacterium tuberculosis.

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Citation

Kefala G, Janowski R, Panjikar S, Mueller-Dieckmann C, Weiss MS

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapB (Rv2773c) from Mycobacterium tuberculosis.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt 7):718-21. Epub 2005 Jun 30.

PubMed ID
16511139 [ View in PubMed
]
Abstract

Dihydrodipicolinate reductase from Mycobacterium tuberculosis (DapB, DHDPR, Rv2773c) has been cloned and heterologously expressed in Escherichia coli, purified using standard chromatographic techniques and crystallized in three different crystal forms. Preliminary diffraction data analysis suggests the presence of two tetramers in the asymmetric unit of one crystal form and half a tetramer in the other two crystal forms.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
4-hydroxy-tetrahydrodipicolinate reductaseP9WP23Details