Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase

Michelle N. Ngamelue, Kohei Homma, Oksana Lockridge, Oluwatoyin A. Asojo

Research output: Contribution to journalArticlepeer-review

56 Scopus citations


Human butyrylcholinesterase (BChE) has been shown to function as an endogenous scavenger of diverse poisons. BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l -1. The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE. In order to be therapeutically useful, BChE must have a long circulatory residence time or associate as tetramers. Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein. Based on the preceding observation as well as the need to develop novel methodologies to facilitate the mass production of therapeutic recombinant BChE, studies have been initiated to determine the structural basis of tetramer formation. Towards these ends, full-length monomeric recombinant BChE has been crystallized for the first time. A 2.8 Å X-ray structure was solved in space group P4212, with unit-cell parameters a = b = 156, c = 146 Å.

Original languageEnglish (US)
Pages (from-to)723-727
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number9
StatePublished - Aug 10 2007


  • BChE
  • Recombinant butyrylcholinesterase
  • Tetramerization domain

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


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