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Nanoflow electrospinning serial femtosecond crystallography.


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.

SUBMITTER: Sierra RG 

PROVIDER: S-EPMC3478121 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature

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Nanoflow electrospinning serial femtosecond crystallography.

Sierra Raymond G RG   Laksmono Hartawan H   Kern Jan J   Tran Rosalie R   Hattne Johan J   Alonso-Mori Roberto R   Lassalle-Kaiser Benedikt B   Glöckner Carina C   Hellmich Julia J   Schafer Donald W DW   Echols Nathaniel N   Gildea Richard J RJ   Grosse-Kunstleve Ralf W RW   Sellberg Jonas J   McQueen Trevor A TA   Fry Alan R AR   Messerschmidt Marc M MM   Miahnahri Alan A   Seibert M Marvin MM   Hampton Christina Y CY   Starodub Dmitri D   Loh N Duane ND   Sokaras Dimosthenis D   Weng Tsu-Chien TC   Zwart Petrus H PH   Glatzel Pieter P   Milathianaki Despina D   White William E WE   Adams Paul D PD   Williams Garth J GJ   Boutet Sébastien S   Zouni Athina A   Messinger Johannes J   Sauter Nicholas K NK   Bergmann Uwe U   Yano Junko J   Yachandra Vittal K VK   Bogan Michael J MJ  

Acta crystallographica. Section D, Biological crystallography 20121018 Pt 11


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 consumptio  ...[more]

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