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.
| Original language | English |
|---|---|
| Pages (from-to) | 718-721 |
| Number of pages | 4 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 61 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - Jul 2005 |
| Externally published | Yes |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
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