Abstract
In the course of protein-structure determinations of the membrane-bound enzyme monoamine oxidase B (MAO B) by X-ray crystallography, a compound was found in the active site of the enzyme that consists of two phenyl rings separated by four C atoms. This compound was identified by chromatography and by mass spectrometry to be 1,4-diphenyl-2-butene and found to be a component of the polystyrene microbridges that are used in protein crystallization. This compound is present at a level of ∼0.3 mg (∼1.5 μmol) per microbridge and functions as a competitive inhibitor of MAO B with a K i of 35 μM. The presence of detergents in the crystallization solutions facilitates the extraction of this compound from the polymer medium.
Original language | English (US) |
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Pages (from-to) | 1874-1876 |
Number of pages | 3 |
Journal | Acta Crystallographica - Section D Biological Crystallography |
Volume | 59 |
Issue number | 10 |
DOIs | |
State | Published - Oct 1 2003 |
ASJC Scopus subject areas
- Structural Biology