4ET9

High-resolution protein structure determination by serial femtosecond crystallography.

Boutet, S., Lomb, L., Williams, G.J., Barends, T.R., Aquila, A., Doak, R.B., Weierstall, U., DePonte, D.P., Steinbrener, J., Shoeman, R.L., Messerschmidt, M., Barty, A., White, T.A., Kassemeyer, S., Kirian, R.A., Seibert, M.M., Montanez, P.A., Kenney, C., Herbst, R., Hart, P., Pines, J., Haller, G., Gruner, S.M., Philipp, H.T., Tate, M.W., Hromalik, M., Koerner, L.J., van Bakel, N., Morse, J., Ghonsalves, W., Arnlund, D., Bogan, M.J., Caleman, C., Fromme, R., Hampton, C.Y., Hunter, M.S., Johansson, L.C., Katona, G., Kupitz, C., Liang, M., Martin, A.V., Nass, K., Redecke, L., Stellato, F., Timneanu, N., Wang, D., Zatsepin, N.A., Schafer, D., Defever, J., Neutze, R., Fromme, P., Spence, J.C., Chapman, H.N., Schlichting, I.

(2012) Science 337: 362-364

• PubMed: 22653729 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1126/science.1217737
• Primary Citation of Related Structures:  
  4ET8, 4ET9, 4ETA, 4ETB, 4ETC, 4ETD, 4ETE


• PubMed 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.

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Organizational Affiliation: 

Linac Coherent Light Source, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, CA 94025, USA. sboutet@slac.stanford.edu