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OSCE Office in Tajikistan donates audio-visual material to enhance interactive teaching at Police Academy

DUSHANBE, 29 July 2016 – The OSCE Office in Tajikistan today donated audio-visual equipment to the Police Academy of Tajikistan’s Ministry of Internal Affairs with the aim of supporting the Academy’s lecturers to use interactive teaching techniques on the investigation of crimes related to the trafficking of human beings.

The equipment includes a computer, a projector, a screen, speakers, a printer, and an Uninterruptible Power Supply device (UPS). An external hard disk drive was also donated to allow for the storing of an electronic library of thematic video films and other informational resources in this field.

“This equipment will improve the teaching of the Course on Combating Trafficking in Human Beings, and will therefore enable the police to more effectively address this serious social problem,” said Fabio Piana, Deputy Head of the OSCE Office in Tajikistan.

Karim Soliev, the first Deputy Director of the Police Academy, thanked the OSCE for its continued support in building the capacity of future law enforcement staff and Police Academy cadets in combating human trafficking and domestic violence in Tajikistan. “This equipment is of great help to lecturers who will now be able to apply more interactive teaching techniques,” he said.

In previous years, the OSCE has provided expert support to the Police Academy, including the development of the Lecturer’s Guidelines on teaching this specialized and compulsory 20-hour course. The OSCE has also trained the team of lecturers on modern interactive teaching techniques and has recently updated the Course on Combating Trafficking in Human Beings with regard to new legislation in this field.

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Characterization of novel mevalonate kinases from the tardigrade Ramazzottius varieornatus and the psychrophilic archaeon Methanococcoides burtonii

Mevalonate kinase is central to the isoprenoid biosynthesis pathway. Here, high-resolution X-ray crystal structures of two mevalonate kinases are presented: a eukaryotic protein from Ramazzottius varieornatus and an archaeal protein from Methanococcoides burtonii. Both enzymes possess the highly conserved motifs of the GHMP enzyme superfamily, with notable differences between the two enzymes in the N-terminal part of the structures. Biochemical characterization of the two enzymes revealed major differences in their sensitivity to geranyl pyrophosphate and farnesyl pyrophosphate, and in their thermal stabilities. This work adds to the understanding of the structural basis of enzyme inhibition and thermostability in mevalonate kinases.