Journal
IUCRJ
Volume 2, Issue -, Pages 545-551Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2052252515013160
Keywords
serial femtosecond crystallography; X-ray free-electron laser; lipidic cubic phase; soluble protein
Funding
- NIH/NIGMS [R01 GM108635]
- Center for Applied Structural Discovery (CASD) at the Biodesign Institute at ASU
- NSF Science and Technology Center [1231306]
- Helmholtz Association
- German Research Foundation (DFG) Cluster of Excellence 'Center for Ultrafast Imaging'
- German Federal Ministry of Education and Research (BMBF) [FKZ 05K12CH1]
- Marie Curie Initial Training Network NanoMem [317079]
- US Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
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Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) enables high-resolution protein structure determination using micrometre-sized crystals at room temperature with minimal effects from radiation damage. SFX requires a steady supply of microcrystals intersecting the XFEL beam at random orientations. An LCP-SFX method has recently been introduced in which microcrystals of membrane proteins are grown and delivered for SFX data collection inside a gel-like membrane-mimetic matrix, known as lipidic cubic phase (LCP), using a special LCP microextrusion injector. Here, it is demonstrated that LCP can also be used as a suitable carrier medium for microcrystals of soluble proteins, enabling a dramatic reduction in the amount of crystallized protein required for data collection compared with crystals delivered by liquid injectors. High-quality LCP-SFX data sets were collected for two soluble proteins, lysozyme and phycocyanin, using less than 0.1 mg of each protein.
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