Malaria research identifies new molecule with therapeutic potential NatureComms
Prior to in vitro motility, PfMyoA was spun at 350,000 ×spin for 20 min in the presence of 1.5 mM MgATP and a three-fold molar excess of skeletal actin. Solutions were added to a nitrocellulose-coated flow cell in 15 µl volumes in the following order. 0.5 mg/ml biotinylated bovine serum albumin in buffer A was incubated for 1 min. 0.7 mg/ml BSA in buffer A was then incubated for 2 min. Neutravidin in buffer A was added for 1 min and rinsed out with three additions of buffer A.
Actin binding to myosin was measured with a modified in vitro motility assay. For visualization in apo, ADP or ATP buffers, motility buffer B that contained either no nucleotide, 2 mM MgADP or 2 mM MgATP without methylcellulose was added after the rhodamine-phalloidin actin binding step. The number of actin filaments bound was quantified manually. Conditions: 25 mM imidazole pH 7.5, 150 mM KCl, 4 mM MgCl, 1 mM EGTA, 10 mM DTT, 0% methylcellulose, 1% DMSO, 30 °C.
Full-length PfMyoA with bound light chains PfELC and MTIP-ΔN was co-crystallized with or without KNX-002. PfMyoA/ELC/ MTIP-ΔN at 10.6 mg/ml was incubated with 2 mM Mg.ADP-gamma-S for 20 min . PfMyoA-KNX-002 crystals were obtained with and without the incubation of 2 mM Mg.ADP-gamma-S for 20 min and 0.5 mM KNX-002 for 40 min. All the samples were centrifugated at 11,000 ×for 15 min at 4 °C before crystallizing assays.
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