Open AccessConcentrated protein solutions investigated using acoustic levitation and small‐angle X‐ray scattering
Author(s) -
Sønderby Pernille,
Söderberg Christopher,
Frankær Christian G.,
Peters Günther,
Bukrinski Jens T.,
Labrador Ana,
Plivelic Tomás S.,
Harris Pernille
Publication year - 2020
Publication title -
journal of synchrotron radiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 99
ISSN - 1600-5775
DOI - 10.1107/s1600577519016977
Subject(s) - small angle x ray scattering , levitation , synchrotron , scattering , capillary action , materials science , ionic strength , analytical chemistry (journal) , sample (material) , work (physics) , chemistry , chromatography , physics , optics , thermodynamics , composite material , aqueous solution , quantum mechanics , magnet
An acoustically levitated droplet has been used to collect synchrotron SAXS data on human serum albumin protein solutions up to a protein concentration of 400 mg ml −1 . A careful selection of experiments allows for fast data collection of a large amount of data, spanning a protein concentration/solvent concentration space with limited sample consumption (down to 3 µL per experiment) and few measurements. The data analysis shows data of high quality that are reproducible and comparable with data from standard flow‐through capillary‐based experiments. Furthermore, using this methodology, it is possible to achieve concentrations that would not be accessible by conventional cells. The protein concentration and ionic strength parameter space diagram may be covered easily and the amount of protein sample is significantly reduced (by a factor of 100 in this work). Used in routine measurements, the benefits in terms of protein cost and time spent are very significant.