BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//CERN//INDICO//EN
BEGIN:VEVENT
SUMMARY:Short Talk 10\, Hongyi Xu - Solving the First Novel Protein Struct
 ure by Micro-Crystal Electron Diffraction
DTSTART;VALUE=DATE-TIME:20191011T074000Z
DTEND;VALUE=DATE-TIME:20191011T080000Z
DTSTAMP;VALUE=DATE-TIME:20260526T060932Z
UID:indico-contribution-771@lindico453.srv.lu.se
DESCRIPTION:Speakers: Hongyi Xu (Stockholm University)\nMicro-crystal elec
 tron diffraction (MicroED) has shown in recent years to be a promising met
 hod for determining\nmacromolecular structures (1–5). It enables structu
 ral biologists to study proteins from micron-sized\n3D crystals that are t
 oo small to be studied by conventional X-ray crystallography. Furthermore\
 , MicroED\ncan be applied to biomolecules of low molecular weight that are
  beyond what can so far be resolved by single\nparticle cryo-EM (6\,7). Ho
 wever\, up to now\, all protein structures determined by MicroED had alrea
 dy been\nsolved previously by X-ray crystallography. Here\, we present for
  the first time an unknown protein structure\n– an R2lox metalloenzyme
 – solved using MicroED (8). MicroED data were collected from plate-like 
 crystals\nwith an average size of 2 μm × 2 μm × 0.5 μm. By overcoming
  challenges in sample handling\, cryo-EM specimen\npreparation\, limited d
 ata completeness and low signal-to-noise ratio\, we are able to solve the 
 structure\nby molecular replacement with a search model of less than 36% s
 equence identity. The resulting electrostatic\nscattering potential map at
  3.0 Å resolution is of sufficient quality to allow accurate model buildi
 ng and refinement\,\nproviding biologically relevant information on the en
 zyme. Our results demonstrate MicroED can be\nused for solving novel prote
 in structures\, using only standard X-ray crystallography software. These 
 findings\nillustrate that electron crystallography has the potential to be
 come a widely applicable tool for revealing new\ninsights into protein str
 ucture and function\, opening up new opportunities for structural biologis
 ts.\n\nRefrences\n1. Shi\, D.\, Nannenga\, B. L.\, Iadanza\, M. G. & Gonen
 \, T. eLife 2\, (2013).\n2. Nannenga\, B. L.\, Shi\, D.\, Leslie\, A. G. W
 . & Gonen\, T. Nat. Methods 11\, 927–930 (2014).\n3. Yonekura\, K.\, Kat
 o\, K.\, Ogasawara\, M.\, Tomita\, M. & Toyoshima\, C. Proc. Natl. Acad. S
 ci. 112\, 3368–3373\n(2015).\n4. Clabbers\, M. T. B. et al. Acta Crystal
 logr. Sect. Struct. Biol. 73\, 738–748 (2017).\n5. Xu\, H. et al. Struct
 ure\, 26\, 667-675 (2018).\n6. Khoshouei\, M.\, Radjainia\, M.\, Baumeiste
 r\, W. & Danev\, R. Nat. Commun. 8\, 16099 (2017).\n7. Henderson\, R. Q. R
 ev. Biophys. 28\, 171 (1995).\n8. Xu\, H. et al. Sci. Adv. 5\, eaax4621 (2
 019).\n\nhttps://lindico453.srv.lu.se/event/125/contributions/771/
LOCATION:Kulturen Auditorium
URL:https://lindico453.srv.lu.se/event/125/contributions/771/
END:VEVENT
END:VCALENDAR