Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 3 (March 2008)

crystallization communications

Acta Cryst. (2008). F64, 182-185 [ doi:10.1107/S174430910800345X ]

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of variants of monoamine oxidase from Aspergillus niger

K. E. Atkin, R. Reiss, N. J. Turner, A. M. Brzozowski and G. Grogan

Abstract: Monoamine oxidase from Aspergillus niger (MAO-N) is an FAD-dependent enzyme that catalyses the conversion of terminal amines to their corresponding aldehydes. Variants of MAO-N produced by directed evolution have been shown to possess altered substrate specificity. Crystals of two of these variants (MAO-N-3 and MAO-N-5) have been obtained; the former displays P2₁ symmetry with eight molecules per asymmetric unit and the latter has P4₁2₁2 or P4₃2₁2 symmetry and two molecules per asymmetric unit. Solution of these structures will help shed light on the molecular determinants of improved activity and high enantioselectivity towards a broad range of substrates.

Keywords: monoamine oxidase; Aspergillus niger; directed evolution; enantioselectivity.