Nanoflow electrospinning serial femtosecond crystallography. Sierra, R. G., Laksmono, H., Kern, J., Tran, R., Hattne, J., Alonso-Mori, R., Lassalle-Kaiser, B., Glöckner, C., Hellmich, J., Schafer, D. W., Echols, N., Gildea, R. J., Grosse-Kunstleve, R. W., Sellberg, J., McQueen, T. A., Fry, A. R., Messerschmidt, M. M., Miahnahri, A., Seibert, M. M., Hampton, C. Y., Starodub, D., Loh, N. D., Sokaras, D., Weng, T., Zwart, P. H., Glatzel, P., Milathianaki, D., White, W. E., Adams, P. D., Williams, G. J., Boutet, S., Zouni, A., Messinger, J., Sauter, N. K., Bergmann, U., Yano, J., Yachandra, V. K., & Bogan, M. J. Acta Crystallographica Section D: Biological Crystallography, 68(11):1584–1587, November, 2012. Publisher: International Union of Crystallography![Nanoflow electrospinning serial femtosecond crystallography [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex An electrospun liquid microjet has been developed that delivers protein microcrystal suspensions at flow rates of 0.14–3.1 µl min−1 to perform serial femtosecond crystallography (SFX) studies with X-ray lasers. Thermolysin microcrystals flowed at 0.17 µl min−1 and diffracted to beyond 4 Å resolution, producing 14 000 indexable diffraction patterns, or four per second, from 140 µg of protein. Nanoflow electrospinning extends SFX to biological samples that necessitate minimal sample consumption.
@article{sierra_nanoflow_2012,
title = {Nanoflow electrospinning serial femtosecond crystallography},
volume = {68},
issn = {0907-4449},
url = {https://journals.iucr.org/d/issues/2012/11/00/lv5021/},
doi = {10.1107/S0907444912038152},
abstract = {An electrospun liquid microjet has been developed that delivers protein microcrystal suspensions at flow rates of 0.14–3.1 µl min−1 to perform serial femtosecond crystallography (SFX) studies with X-ray lasers. Thermolysin microcrystals flowed at 0.17 µl min−1 and diffracted to beyond 4 Å resolution, producing 14 000 indexable diffraction patterns, or four per second, from 140 µg of protein. Nanoflow electrospinning extends SFX to biological samples that necessitate minimal sample consumption.},
language = {en},
number = {11},
urldate = {2024-12-10},
journal = {Acta Crystallographica Section D: Biological Crystallography},
author = {Sierra, R. G. and Laksmono, H. and Kern, J. and Tran, R. and Hattne, J. and Alonso-Mori, R. and Lassalle-Kaiser, B. and Glöckner, C. and Hellmich, J. and Schafer, D. W. and Echols, N. and Gildea, R. J. and Grosse-Kunstleve, R. W. and Sellberg, J. and McQueen, T. A. and Fry, A. R. and Messerschmidt, M. M. and Miahnahri, A. and Seibert, M. M. and Hampton, C. Y. and Starodub, D. and Loh, N. D. and Sokaras, D. and Weng, T.-C. and Zwart, P. H. and Glatzel, P. and Milathianaki, D. and White, W. E. and Adams, P. D. and Williams, G. J. and Boutet, S. and Zouni, A. and Messinger, J. and Sauter, N. K. and Bergmann, U. and Yano, J. and Yachandra, V. K. and Bogan, M. J.},
month = nov,
year = {2012},
note = {Publisher: International Union of Crystallography},
pages = {1584--1587},
}
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