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!

TimePresenterPresentation title
13.00Joachim Schnadt, MAX IV LaboratoryIntroduction & Overview
13.15Samuli Urpelainen, MAX IV LaboratoryThe SPECIES beamline
13.35Jan Knudsen, MAX IV LaboratoryThe HIPPIE beamline
13.55Break
14.00Håkan Rensmo, Uppsala UniversityStudies on Energy and Enviornmental Applications using X-ray-based Spectroscopy
14.20Rainer Timm, Lund UniversityUnexpected surface chemistry during atomic layer deposition of high-k oxides revealed by time-resolved XPS
14.40Harri Ali-LöyttyX-ray photoelectron spectroscopy of electrochemical interfaces for solar fuel production
15.00Coffee break
15.30Peter Amann, Stockholm UniversityAmbient Pressure XPS at Stockholm University
15.50Jeppe Vang Lauritsen, Aarhus UniversityAmbient pressure studies of sulfide catalysts
16.10Jens Uhlig, Lund UniversityHPXPS for electron dynamics
16.30Dmytro Orlov(Bio-)Degradation of Mg alloys as a hot subject for ambient pressure XPS studies
16.50Break
17.00Visit of the HIPPIE and SPECIES beamlines

2021-10-06

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