Crystallization and preliminary X-ray crystallographic analysis of the electron-transferring flavoprotein from Megasphaera elsdenii

Timothy Martin Higgins

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Abstract

Electron-transferring flavoprotein from the rumen bacterium Megasphaera elsdenii is a heterodimer (M-r = 75 kDa) containing FAD as cofactor and functioning solely to mediate electron transfer between the prosthetic groups of other proteins. The enzyme was crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 4000 as precipitant. The crystals obtained belong to the space group P2(1)2(1)2(1) with unit-cell dimensions of a = 58.75, b = 61.77 and c = 122.27 Angstrom. Interestingly the crystals exhibit a low solvent content. Crystals diffracted to beyond 2.5 Angstrom using synchrotron radiation.
Original languageEnglish (Ireland)
Number of pages3
JournalACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Volume53
Publication statusPublished - 1 Jul 1997

Authors (Note for portal: view the doc link for the full list of authors)

  • Authors
  • Sharkey, CT,Walsh, MA,Mayhew, SG,Higgins, TM

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