BEGIN:VCALENDAR
VERSION:2.0
PRODID:icalendar-ruby
CALSCALE:GREGORIAN
METHOD:PUBLISH
BEGIN:VTIMEZONE
TZID:Europe/Vienna
BEGIN:DAYLIGHT
DTSTART:20250330T030000
TZOFFSETFROM:+0100
TZOFFSETTO:+0200
RRULE:FREQ=YEARLY;BYDAY=-1SU;BYMONTH=3
TZNAME:CEST
END:DAYLIGHT
BEGIN:STANDARD
DTSTART:20251026T020000
TZOFFSETFROM:+0200
TZOFFSETTO:+0100
RRULE:FREQ=YEARLY;BYDAY=-1SU;BYMONTH=10
TZNAME:CET
END:STANDARD
END:VTIMEZONE
BEGIN:VEVENT
DTSTAMP:20260424T102228Z
UID:1755176400@ist.ac.at
DTSTART:20250814T150000
DTEND:20250814T160000
DESCRIPTION:Speaker: Jakob Vorlaufer\nhosted by Georgios Katsaros\nAbstract
 : The internal structure of biomolecules and their organization in higher-
 order arrangements are key factors governing the working principles of bio
 logical systems. Bioimaging has successfully revealed arrangements across 
 relevant spatial scales. For example\, cryo-electron tomography has become
  widely used for analyzing biomolecular structures in situ due to its comp
 rehensive structural visualization of near-natively preserved samples\, an
 d its capability of sub-nm resolution via averaging. However\, the identif
 ication of molecules withing crowded cellular environments is often hinder
 ed by low contrast. Fluorescence microscopy\, on the other hand\, routinel
 y visualizes specifically labeled targets at single-molecule contrast agai
 nst essentially zero background. Moreover\, it provides comparatively high
  throughput and is amenable to multiplexing. Due to this complementarity\,
  combining datasets from both modalities acquired on the same region via c
 orrelative light and electron microscopy can reveal novel types of informa
 tion. The spatial scale at which information can be extracted depends on 
 imaging resolution and correlation accuracy. Since diffraction of light li
 mits the resolution of conventional fluorescence microscopy to few hundred
 s of nanometers\, reaching the full potential of correlative imaging requi
 res super-resolution approaches. Performing imaging at cryogenic temperatu
 re preserves structures in a near-native state and minimizes distortions b
 etween the fluorescence and the electron microscopy datasets. Implementati
 ons of this concept have achieved correlation on the scale of cellular org
 anelles or bacterial domains.We have worked towards pushing correlative im
 aging to the single-molecule scale by improving cryo-super-resolution micr
 oscopy\, and devising a refined image correlation workflow. As part of thi
 s project\, I constructed a microscopy setup and adopted it for super-reso
 lution fluorescence microscopy at room temperature and cryogenic condition
 s. I explored different cryo-stages and acquisition strategies. Specifical
 ly\, I developed a new scheme for correcting sample drift\, thus increasin
 g mechanical stability during microscopy acquisitions.
LOCATION:Moonstone Bldg / Ground floor / Seminar Room G (I24.EG.030g) and Z
 oom\, ISTA
ORGANIZER:
SUMMARY:Jakob Vorlaufer: Thesis Defense: Construction of a cryo-super-resol
 ution microscope to guide in situ structure analysis
URL:https://talks-calendar.ista.ac.at/events/5944
END:VEVENT
END:VCALENDAR