Nanoflow electrospinning serial femtosecond crystallography

Sierra, Raymond G.; Laksmono, Hartawan; Kern, Jan; Tran, Rosalie; Hattne, Johan; Alonso-Mori, Roberto; Lassalle‐Kaiser, Benedikt; Glöckner, Carina; Hellmich, Julia; Schafer, Donald W.; Echols, Nathaniel; Gildea, Richard J.; Grosse‐Kunstleve, Ralf W.; Sellberg, Jonas A.; McQueen, Trevor A.; Fry, Alan; Messerschmidt, Marc; Miahnahri, Alan; Seibert, M.; Hampton, Christina Y.; Starodub, D.; Loh, N. Duane; Sokaras, Dimosthenis; Weng, Tsu Chien; Zwart, Petrus H.; Glatzel, Pieter; Milathianaki, Despina; White, William E.; Adams, Paul D.; Williams, Garth J.; Boutet, Sébastien; Zouni, Athina; Messinger, Johannes; Sauter, Nicholas K.; Bergmann, Uwe; Yano, Junko; Yachandra, Vittal K.; Bogan, Michael J.

doi:10.1107/s0907444912038152

Cited by 175 publications

(175 citation statements)

References 22 publications

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“…However, the slow running jet is problematic for TR-SFX experiments. Another jet type has been reported by Bogan and co-workers [20] which is based on electrospinning and also allows for the use of larger crystals; however, not all crystals may survive this procedure and the hit rates reported for use of this injector are very low.…”

Section: Discussion (A) Batch Methodsmentioning

confidence: 99%

“…Alternative injector designs, with lower flow rates have also been developed; however, they require proteins to be delivered in highly viscous media. They include the injector described by Sierra et al [20] that delivers proteins by electrospinning and the recent development of a novel injector design that allows delivery of protein crystals in lipidic cubic phase [21].…”

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confidence: 99%

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Microcrystallization techniques for serial femtosecond crystallography using photosystem II from Thermosynechococcus elongatus as a model system

Kupitz

Grotjohann

Conrad

et al. 2014

Phil. Trans. R. Soc. B

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Serial femtosecond crystallography (SFX) is a new emerging method, where X-ray diffraction data are collected from a fully hydrated stream of nano-or microcrystals of biomolecules in their mother liquor using high-energy, X-ray free-electron lasers. The success of SFX experiments strongly depends on the ability to grow large amounts of well-ordered nano/microcrystals of homogeneous size distribution. While methods to grow large single crystals have been extensively explored in the past, method developments to grow nano/ microcrystals in sufficient amounts for SFX experiments are still in their infancy. Here, we describe and compare three methods (batch, free interface diffusion (FID) and FID centrifugation) for growth of nano/microcrystals for time-resolved SFX experiments using the large membrane protein complex photosystem II as a model system.

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Section: Discussion (A) Batch Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Microcrystallization techniques for serial femtosecond crystallography using photosystem II from Thermosynechococcus elongatus as a model system

Kupitz

Grotjohann

Conrad

et al. 2014

Phil. Trans. R. Soc. B

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“…The collection of serial crystallography data has been described in detail elsewhere and can be accomplished in a range of ways including using flowing liquid suspensions [13], electrospinning [14], viscous extrusion [15,16] and fixed targets [14,17]. Diffraction data can be measured using either X-ray Free Electron Laser [1,2,15,18] or Synchrotron [9,19,20] sources.…”

Section: Data Collection and Initial Processingmentioning

confidence: 99%

Accurate determination of segmented X-ray detector geometry

Yefanov¹,

Mariani²,

Gati³

et al. 2015

Opt. Express

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Recent advances in X-ray detector technology have resulted in the introduction of segmented detectors composed of many small detector modules tiled together to cover a large detection area. Due to mechanical tolerances and the desire to be able to change the module layout to suit the needs of different experiments, the pixels on each module might not align perfectly on a regular grid. Several detectors are designed to permit detector sub-regions (or modules) to be moved relative to each other for different experiments. Accurate determination of the location of detector elements relative to the beam-sample interaction point is critical for many types of experiment, including X-ray crystallography, coherent diffractive imaging (CDI), small angle X-ray scattering (SAXS) and spectroscopy. For detectors with moveable modules, the relative positions of pixels are no longer fixed, necessitating the development of a simple procedure to calibrate detector geometry after reconfiguration. We describe a simple and robust method for determining the geometry of segmented X-ray detectors using measurements obtained by serial crystallography. By comparing the location of observed Bragg peaks to the spot locations predicted from the crystal indexing procedure, the position, rotation and distance of each module relative to the interaction region can be refined. We show that the refined detector geometry greatly improves the results of experiments. #245734Received 17 Boutet, M. Messerschmidt, and I. Schlichting, "De novo protein crystal structure determination from X-ray freeelectron laser data," Nature 505(7482), 244-247 (2013). 23. M. Schmidt, K. Pande, S. Basu, and J. Tenboer, "Room temperature structures beyond 1.5 Å by serial femtosecond crystallography," Struct. Dyn. 2(4), 041708 (2015).

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“…Redecke et al, 2013;Kang et al, 2015) and time-resolved studies of light-triggered reactions (Tenboer et al, 2014;Barends et al, 2015). Although recent developments in sample injection methods (Sierra et al, 2012;Weierstall et al, 2014;Sugahara et al, 2015) and data processing algorithms (White, 2014;White et al, 2016;Sauter, 2015;Uervirojnangkoorn et al, 2015;Ginn et al, 2015) have reduced the number of crystals, the amount of time and the quantity of data necessary for structure solution, thousands to tens of thousands of high-resolution diffraction patterns are still required to obtain an accurate data set.…”

Section: Introductionmentioning

confidence: 99%

Data processing pipeline for serial femtosecond crystallography at SACLA

et al. 2016

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A data processing pipeline for serial femtosecond crystallography at SACLA was developed, based on Cheetah [Barty et al. (2014). J. Appl. Cryst. 47, 1118-1131] and CrystFEL [White et al. (2016). J. Appl. Cryst. 49, 680-689]. The original programs were adapted for data acquisition through the SACLA API, thread and inter-node parallelization, and efficient image handling. The pipeline consists of two stages: The first, online stage can analyse all images in real time, with a latency of less than a few seconds, to provide feedback on hit rate and detector saturation. The second, offline stage converts hit images into HDF5 files and runs CrystFEL for indexing and integration. The size of the filtered compressed output is comparable to that of a synchrotron data set. The pipeline enables real-time feedback and rapid structure solution during beamtime.

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Nanoflow electrospinning serial femtosecond crystallography

Cited by 175 publications

References 22 publications

Microcrystallization techniques for serial femtosecond crystallography using photosystem II from Thermosynechococcus elongatus as a model system

Microcrystallization techniques for serial femtosecond crystallography using photosystem II from Thermosynechococcus elongatus as a model system

Accurate determination of segmented X-ray detector geometry

Data processing pipeline for serial femtosecond crystallography at SACLA

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