Minisymposium on Ambient pressure x-ray photoelectron spectroscopy at MAX IV
On Monday, 30 May 2016, a minisymposium on “Ambient pressure x-ray photoelectron spectroscopy at MAX IV” was held at the MAX IV Laboratory. The minisymposium had the aim to provide an opportunity to discuss the status of the SPECIES and HIPPIE beamlines at MAX IV as well as current and future science with Ambient pressure x-ray photoelectron spectroscopy (APXPS). Please find the programme of the minisymposium below. Presentations available to us will soon be published here.
We would like to thank all speakers for their excellent contributions – due to these contributions the Ambient pressure x-ray photoelectron spectroscopy became a very inspiring and successful event!
|13.00||Joachim Schnadt, MAX IV Laboratory||Introduction & Overview|
|13.15||Samuli Urpelainen, MAX IV Laboratory||The SPECIES beamline|
|13.35||Jan Knudsen, MAX IV Laboratory||The HIPPIE beamline|
|14.00||Håkan Rensmo, Uppsala University||Studies on Energy and Enviornmental Applications using X-ray-based Spectroscopy|
|14.20||Rainer Timm, Lund University||Unexpected surface chemistry during atomic layer deposition of high-k oxides revealed by time-resolved XPS|
|14.40||Harri Ali-Löytty||X-ray photoelectron spectroscopy of electrochemical interfaces for solar fuel production|
|15.30||Peter Amann, Stockholm University||Ambient Pressure XPS at Stockholm University|
|15.50||Jeppe Vang Lauritsen, Aarhus University||Ambient pressure studies of sulfide catalysts|
|16.10||Jens Uhlig, Lund University||HPXPS for electron dynamics|
|16.30||Dmytro Orlov||(Bio-)Degradation of Mg alloys as a hot subject for ambient pressure XPS studies|
|17.00||Visit of the HIPPIE and SPECIES beamlines|
First Mce4A structure of Mycobacterium tuberculosis – revealed at BioMAX
The crystal structure of MtMce4A39–140 shows four molecules in asymmetric units. The structure of the substrate-binding mammalian cell entry (Mce)4A protein from Mycobacterium tuberculosis, the causative agent of the disease Tuberculosis, was unknown — until recent research at BioMAX beamline. It showed the unique Mce domain of Mce4A, a part of the cholesterol importing complex of