纳米晶材料
蛋白质结晶
纳米晶
无定形固体
纳米结构
材料科学
核糖核酸酶P
结晶学
蛋白质结构
他马汀
纳米技术
化学
结晶
生物化学
核糖核酸
有机化学
基因
作者
Daniel G. Greene,Shannon Modla,Stanley I. Sandler,Norman J. Wagner,Abraham M. Lenhoff
标识
DOI:10.1107/s2053230x21009961
摘要
Protein salting-out is a well established phenomenon that in many cases leads to amorphous structures and protein gels, which are usually not considered to be useful for protein structure determination. Here, microstructural measurements of several different salted-out protein dense phases are reported, including of lysozyme, ribonuclease A and an IgG1, showing that salted-out protein gels unexpectedly contain highly ordered protein nanostructures that assemble hierarchically to create the gel. The nanocrystalline domains are approximately 10–100 nm in size, are shown to have structures commensurate with those of bulk crystals and grow on time scales in the order of an hour to a day. Beyond revealing the rich, hierarchical nanoscale to mesoscale structure of protein gels, the nanocrystals that these phases contain are candidates for structural biology on next-generation X-ray free-electron lasers, which may enable the study of biological macromolecules that are difficult or impossible to crystallize in bulk.
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