High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography Academic Article uri icon

abstract

  • Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.

authors

  • Boutet, S
  • Lomb, L
  • Williams, GJ
  • Barends, TRM
  • Aquila, A
  • Doak, RB
  • Weierstall, U
  • DePonte, DP
  • Steinbrener, J
  • Shoeman, RL
  • Messerschmidt, M
  • Barty, A
  • White, TA
  • Kassemeyer, S
  • Kirian, RA
  • Seibert, MM
  • Montanez, PA
  • Kenney, C
  • Herbst, R
  • Hart, P
  • Pines, J
  • Haller, G
  • Gruner, SM
  • Philipp, HT
  • Tate, MW
  • Hromalik, M
  • Koerner, LJ
  • van Bakel, N
  • Morse, J
  • Ghonsalves, W
  • Arnlund, D
  • Bogan, MJ
  • Caleman, C
  • Fromme, R
  • Hampton, CY
  • Hunter, MS
  • Johansson, LC
  • Katona, G
  • Kupitz, C
  • Liang, M
  • Martin, AV
  • Nass, K
  • Redecke, L
  • Stellato, F
  • Timneanu, N
  • Wang, D
  • Zatsepin, NA
  • Schafer, D
  • Defever, J
  • Neutze, R
  • Fromme, P
  • Spence, JCH
  • Chapman, HN
  • Schlichting, I

publication date

  • July 20, 2012