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2 results on '"Sztuk-Dambietz, Jolanta"'

1. Segmented flow generator for serial crystallography at the European X-ray free electron laser.

Author

Echelmeier A, Cruz Villarreal J, Messerschmidt M, Kim D, Coe JD, Thifault D, Botha S, Egatz-Gomez A, Gandhi S, Brehm G, Conrad CE, Hansen DT, Madsen C, Bajt S, Meza-Aguilar JD, Oberthür D, Wiedorn MO, Fleckenstein H, Mendez D, Knoška J, Martin-Garcia JM, Hu H, Lisova S, Allahgholi A, Gevorkov Y, Ayyer K, Aplin S, Ginn HM, Graafsma H, Morgan AJ, Greiffenberg D, Klujev A, Laurus T, Poehlsen J, Trunk U, Mezza D, Schmidt B, Kuhn M, Fromme R, Sztuk-Dambietz J, Raab N, Hauf S, Silenzi A, Michelat T, Xu C, Danilevski C, Parenti A, Mekinda L, Weinhausen B, Mills G, Vagovic P, Kim Y, Kirkwood H, Bean R, Bielecki J, Stern S, Giewekemeyer K, Round AR, Schulz J, Dörner K, Grant TD, Mariani V, Barty A, Mancuso AP, Weierstall U, Spence JCH, Chapman HN, Zatsepin N, Fromme P, Kirian RA, and Ros A

Subjects
Aldehyde-Lyases ultrastructure, Escherichia coli Proteins ultrastructure, Hydrodynamics, Crystallography instrumentation, Electrons, Lab-On-A-Chip Devices, Lasers
Abstract

Serial femtosecond crystallography (SFX) with X-ray free electron lasers (XFELs) allows structure determination of membrane proteins and time-resolved crystallography. Common liquid sample delivery continuously jets the protein crystal suspension into the path of the XFEL, wasting a vast amount of sample due to the pulsed nature of all current XFEL sources. The European XFEL (EuXFEL) delivers femtosecond (fs) X-ray pulses in trains spaced 100 ms apart whereas pulses within trains are currently separated by 889 ns. Therefore, continuous sample delivery via fast jets wastes >99% of sample. Here, we introduce a microfluidic device delivering crystal laden droplets segmented with an immiscible oil reducing sample waste and demonstrate droplet injection at the EuXFEL compatible with high pressure liquid delivery of an SFX experiment. While achieving ~60% reduction in sample waste, we determine the structure of the enzyme 3-deoxy-D-manno-octulosonate-8-phosphate synthase from microcrystals delivered in droplets revealing distinct structural features not previously reported.

Published
2020
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2. Membrane protein megahertz crystallography at the European XFEL.

Author

Gisriel C, Coe J, Letrun R, Yefanov OM, Luna-Chavez C, Stander NE, Lisova S, Mariani V, Kuhn M, Aplin S, Grant TD, Dörner K, Sato T, Echelmeier A, Cruz Villarreal J, Hunter MS, Wiedorn MO, Knoska J, Mazalova V, Roy-Chowdhury S, Yang JH, Jones A, Bean R, Bielecki J, Kim Y, Mills G, Weinhausen B, Meza JD, Al-Qudami N, Bajt S, Brehm G, Botha S, Boukhelef D, Brockhauser S, Bruce BD, Coleman MA, Danilevski C, Discianno E, Dobson Z, Fangohr H, Martin-Garcia JM, Gevorkov Y, Hauf S, Hosseinizadeh A, Januschek F, Ketawala GK, Kupitz C, Maia L, Manetti M, Messerschmidt M, Michelat T, Mondal J, Ourmazd A, Previtali G, Sarrou I, Schön S, Schwander P, Shelby ML, Silenzi A, Sztuk-Dambietz J, Szuba J, Turcato M, White TA, Wrona K, Xu C, Abdellatif MH, Zook JD, Spence JCH, Chapman HN, Barty A, Kirian RA, Frank M, Ros A, Schmidt M, Fromme R, Mancuso AP, Fromme P, and Zatsepin NA

Subjects
Crystallography, Cyanobacteria metabolism, Models, Molecular, Photosystem I Protein Complex chemistry, Photosystem I Protein Complex isolation & purification, Static Electricity, Synchrotrons, Thermosynechococcus, X-Rays, Electrons, Lasers, Membrane Proteins chemistry
Abstract

The world's first superconducting megahertz repetition rate hard X-ray free-electron laser (XFEL), the European XFEL, began operation in 2017, featuring a unique pulse train structure with 886 ns between pulses. With its rapid pulse rate, the European XFEL may alleviate some of the increasing demand for XFEL beamtime, particularly for membrane protein serial femtosecond crystallography (SFX), leveraging orders-of-magnitude faster data collection. Here, we report the first membrane protein megahertz SFX experiment, where we determined a 2.9 Å-resolution SFX structure of the large membrane protein complex, Photosystem I, a > 1 MDa complex containing 36 protein subunits and 381 cofactors. We address challenges to megahertz SFX for membrane protein complexes, including growth of large quantities of crystals and the large molecular and unit cell size that influence data collection and analysis. The results imply that megahertz crystallography could have an important impact on structure determination of large protein complexes with XFELs.

Published
2019
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