Acta Crystallographica Section F

Structural Biology Communications

Volume 70, Part 4 (April 2014)

crystallization communications

Acta Cryst. (2014). F70, 470-472    [ doi:10.1107/S2053230X14004087 ]

Crystallization and preliminary neutron diffraction experiment of human farnesyl pyrophosphate synthase complexed with risedronate

T. Yokoyama, A. Ostermann, M. Mizuguchi, N. Niimura, T. E. Schrader and I. Tanaka

Abstract: Nitrogen-containing bisphosphonates (N-BPs), such as risedronate and zoledronate, are currently used as a clinical drug for bone-resorption diseases and are potent inhibitors of farnesyl pyrophosphate synthase (FPPS). X-ray crystallographic analyses of FPPS with N-BPs have revealed that N-BPs bind to FPPS with three magnesium ions and several water molecules. To understand the structural characteristics of N-BPs bound to FPPS, including H atoms and hydration by water, neutron diffraction studies were initiated using BIODIFF at the Heinz Maier-Leibnitz Zentrum (MLZ). FPPS-risedronate complex crystals of approximate dimensions 2.8 × 2.5 × 1.5 mm (~3.5 mm3) were obtained by repeated macro-seeding. Monochromatic neutron diffraction data were collected to 2.4 Å resolution with 98.4% overall completeness. Here, the first successful neutron data collection from FPPS in complex with N-BPs is reported.

Keywords: neutron protein crystallography; farnesyl pyrophosphate synthase.

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