Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography Academic Article uri icon

abstract

  • Serial femtosecond crystallography is an X-ray free-electron-laser-based method with considerable potential to have an impact on challenging problems in structural biology. Here we present X-ray diffraction data recorded from microcrystals of the Blastochloris viridis photosynthetic reaction centre to 2.8 Å resolution and determine its serial femtosecond crystallography structure to 3.5 Å resolution. Although every microcrystal is exposed to a dose of 33 MGy, no signs of X-ray-induced radiation damage are visible in this integral membrane protein structure.

authors

  • Johansson, LC
  • Arnlund, D
  • Katona, G
  • White, TA
  • Barty, A
  • DePonte, DP
  • Shoeman, RL
  • Wickstrand, C
  • Sharma, A
  • Williams, GJ
  • Aquila, A
  • Bogan, MJ
  • Caleman, C
  • Davidsson, J
  • Doak, RB
  • Frank, M
  • Fromme, R
  • Galli, L
  • Grotjohann, I
  • Hunter, MS
  • Kassemeyer, S
  • Kirian, RA
  • Kupitz, C
  • Liang, M
  • Lomb, L
  • Malmerberg, E
  • Martin, AV
  • Messerschmidt, M
  • Nass, K
  • Redecke, L
  • Seibert, MM
  • Sjohamn, J
  • Steinbrener, J
  • Stellato, F
  • Wang, D
  • Wahlgren, WY
  • Weierstall, U
  • Westenhoff, S
  • Zatsepin, NA
  • Boutet, S
  • Spence, JCH
  • Schlichting, I
  • Chapman, HN
  • Fromme, P
  • Neutze, R

publication date

  • 2013