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Updated: Aug 11, 2026

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit
Published on: June 28, 2013
Cloning, expression, purification and preliminary crystallographic data for Rv3214 (EntD), a predicted
Harriet A Watkins1, MinMin Yu, Edward N Baker
1Centre for Molecular Biodiscovery, School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand. h.watkins@auckland.ac.nz
Abstract:
The Mycobacterium tuberculosis open reading frame Rv3214, annotated as a cofactor-dependent phosphoglycerate mutase, has been cloned and expressed as an N-terminally His-tagged protein. Tagged, untagged and selenomethionine-labelled forms of Rv3214 (EntD) have been purified using nickel-affinity chromatography and gel filtration. The selenomethionine-labelled crystals diffracted to 2.15 A resolution and belong to space group P2(1), with unit-cell parameters a = 44.36, b = 79.03, c = 52.85 A, beta = 109.11 degrees. There are two molecules of molecular weight 21,948 Da per asymmetric unit.

