Abstract
By utilizing their ultra-fast, intense, and highly coherent X-ray pulses, serial femtosecond crystallography (SFX) at X-ray free electron lasers (XFELs) has proven a powerful tool for structural characterization of membrane proteins, which are challenging to crystallize due to solubility and stability obstacles during expression and purification. However, the limitations of both detergents to solubilize membrane proteins in native-like environments, and delivery of the microcrystalline sample into the X-ray beam path while maintaining low X-ray scatter background and with minimal sample consumption, remain technical challenges, especially where this methodology is applied to relatively low-ordered samples or those difficult to purify and crystallize in large quantities.
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