Skip to main content
padlock icon - secure page this page is secure

Cloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of tetrahydrodipicolinate‐N‐succinyltransferase (Rv1201c) from Mycobacterium tuberculosis

Buy Article:

$52.00 + tax (Refund Policy)

Tetrahydrodipicolinate‐N‐succinyltransferase from Mycobacterium tuberculosis (DapD, Rv1201c) has been cloned, heterologously expressed in Escherichia coli, purified using standard chromatographic techniques and crystallized in the cubic space group I23 or I213. Preliminary diffraction data analysis indicates the presence of five molecules per asymmetric unit. Furthermore, the data exhibit icosahedral point‐group symmetry. One possible explanation for this is that the enzyme assembles into a 60‐mer exhibiting 235 point‐group symmetry and crystallizes as such in space group I23. In this case, the combination of crystallographic and noncrystallographic symmetry elements results in an arrangement of the icosahedrons in the cubic crystal with one pentamer in the asymmetric unit. Another explanation is that the packing of the molecules itself mimics icosahedral symmetry. In this case both space groups I23 and I213 would be possible.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: DapD; Mycobacterium tuberculosis; tetrahydrodipicolinate‐N‐succinyltransferase

Document Type: Research Article

Affiliations: EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany

Publication date: September 1, 2008

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more