Editorial: In celebration of women in science: Structural biology

Why do we still have to celebrate women in science, why are women in science not a normality? For decades women have been underrepresented in STEM (science, technology, engineering, andmathematics) at universities and occupations. As a matter of fact only around 30% of researchers globally are female. Despite this huge imbalance, women have given a huge contribute to STEM research in general and to the development of Structural Biology in particular. Women were among structural biology’s earliest pioneers. The work of Rosalind Franklin, a British crystallographer, laid the basis for the understanding of the double helix structure of DNA. Crystallographers are also two of the eight women scientists who won the Nobel prize for Chemistry, Dorothy Hodgkin awarded in 1964 for her pioneering work in X-ray crystallography of biomolecules and Ada Yonath who won it in 2009 for her studies on the structure and function of the ribosome. Structural studies of Cas9 were tremendously important for Jennifer Doudna and Emmanuelle Charpentier who were awarded with the 2020 Chemistry Nobel prize for their work on the gene editing tool CRISPR/Cas9. The works presented in this Research Topic give a small account of the diversity of research performed by women across the entire breadth of Structural Biology research and present, advances in compelling problems like protein aggregation and its connection to tauopathy the design of functional nanomachines for drug delivery, molecular mechanisms of apoptosis, and structural characterization of an animal protein involved in lipid-transport. Lyu et al. compared the structural properties of Tau35 (Wray et al., 2008), a truncated form of tau found in humanbrain in a subset of tauopathies (Guo et al., 2017), with the two longer isoforms 2N3R and 2N4R tau. Using small angle X-ray scattering, they found that Tau35 is more rigid than the other two isoforms. Additionally, Tau35 aggregates more quickly and to a greater extent than full-length tau in the presence of the polyanion heparin, an agent often used in tau studies to induce protein aggregation (Zhang et al., 2019; Lin et al., 2020). Combining several biophysical techniques they show that Tau35 aggregation is similar to previously reported tau fibrils but more densely packed. Their findings provide insight into the aggregation-inducing properties of clinically relevant tau fragments and their role in the pathogenesis of human tauopathies. Protein assemblies can also be used to produce functional nanosystems for drug delivery. Ferritins (Fts) are ubiquitous proteins in nature and very versatile systems for biotechnology applications. The human heavy chain ferritin (hHFt) nanocages are ideal for the delivery of anticancer drugs due to their lack of immunogenicity and selective interaction with tumor cells (Li et al., 2010; Zhen et al., 2013). However, the current protocols for disassembling and reassembling hHFt to load cargomolecules have still some drawbacks, such as low protein recovery (Zhang et al., 2020; Zhang et al., 2021) and homogeneity. Moreover, the exposure to extreme pH during loading OPEN ACCESS