Dr. Jacques Dubochet, Dr. Joachim Frank, and Dr. Richard Henderson received the 2017 Nobel Prize for Chemistry for their efforts to develop effective ways to obtain high-resolution three-dimensional images of biomolecules using cryo-electron microscopy. Congratulations to the Nobel Prize in the field of electron microscopy, I will explain the scientific contributions of the three winners and introduce the role of cryo-electron microscopy (including cryo technology) in biology.

The 2017 Nobel Prize in Chemistry was awarded to the following three pioneers: Dr. Joachim Frank, Dr. Jacques Dubochet, and Dr. Richard Henderson. They all contributed to the development of a Cryo-electron microscopy (EM) technique for determining the high-resolution structures of biomolecules in solution, particularly without crystal and with much less amount of biomolecules than X-ray crystallography. In this brief commentary, we address the major advances made by these three Nobel laureates as well as the current status and future prospects of this Cryo-EM technique.

Cryo-electron microscopy (cryo-EM) is arguably the most powerful tool used in structural biology. It is an important analytical technique that is used for gaining insight into the functional and molecular mechanisms of biomolecules involved in several physiological processes. Cryo-EM can be separated into the following three groups according to the analytical purposes and the features of the biological samples: cryo-electron tomography (cryo-ET), cryo-single-particle reconstruction, and cryo-electron crystallography. Cryo-tomography is a unique EM technique that is used to study intact biomolecular complexes within their original environments; it can provide mechanistic insights that are challenging for other EM-methods. However, the resolution of reconstructed three-dimensional (3D) models generated by cryo-ET is relatively low, while single-particle reconstruction can reproduce biomolecular structures having near-atomic resolution without the need for crystallization unless the samples are large (>200 kDa) and highly symmetrical. Cryo-electron crystallography is subdivided into the following two categories according to the types of samples: one category that deals with two-dimensional (2D) crystalline arrays and the other category that uses 3D crystals. These two categories of electron-crystallographic techniques use different diffraction data obtained from still diffraction and continuous-rotation diffraction. In this paper, we review crystal-based cryo-EM techniques and focus on the recently developed 3D electron-crystallographic technique called microcrystal-electron diffraction.

Electron microscopy and X-ray diffraction have together played a key role in our understanding of the molecular structure and mechanism of contraction of muscle. This review highlights the role of electron microscopy, from early insights into thick and thin filament structure by negative staining, to studies of single myosin molecule structure, and finally to recent high-resolution structures by cryo-electron microscopy. Muscle filaments are designed for movement. Their labile structures thus present challenges to obtaining near-atomic detail, which are also discussed.

Chronic eosinophilic leukemia (CEL) is a myeloproliferative disease with an increased number of mature eosinophils and their precursors, which results in infiltration into organs and organ enlargement. The main cause of this disease is the overexpression of tyrosine kinase. However, there is a need for alternative medication, because some patients are resistant to imatinib, which is a tyrosine kinase inhibitor for leukemia. Many studies have indicated that S100A8 and splicing factor proline and glutamine-rich (SFPQ) function as initiation signals of apoptosis in CEL cells. We reviewed structural studies on CEL cells related to S100A8 and SFPQ. Particularly, this review highlighted microscopic results for the study of S100A8 and SFPQ in CEL cells.

A study on the visual cell and eyeball of the endemic Korean species Liobagrus mediadiposalis was investigated by light and electron microscopes. The retina of a small and 2 mm-diameter round eye was thin, $151.0{\pm}4.0{\mu}m$ and has two visual cells, a single cone and a rod cell. The single cone cells are short and thick, $18.0{\pm}0.9{\mu}m$ in length and $5.1{\pm}0.7{\mu}m$ (n=30) in diameter, while the rod cells are longer and thinner, $54.8{\pm}2.9{\mu}m$ in length and $3.3{\pm}0.6{\mu}m$ in diameter. The cone cells are seen an irregular and random mosaic pattern, and the rod cells are also randomly situated at between cone cells. As a rare phenomenon, such structure is one of characteristics reflecting the eye of a nocturnal and bottom-dwelling freshwater fish. The ultrastructure of visual cells was observed with scanning and transmission electron microscopy, both cone and rod cells are divided into an inner segment with numerous mitochondria and an outer segment with stacks of membrane discs.

The purpose of this study was to characterize the prenatal and postnatal development of the mouse parotid salivary gland and tooth, and to investigate the relationship between the developmental timing of the two organs. Development of parotid salivary gland begins on embryonic day 15 (E15), which is the prebud stage; E17 is the initial bud stage; E21 to postnatal day 3 (PN3) is the pseudoglandular stage; PN5 to PN10 is the canalicular stage; and PN21 is the terminal bud stage. At E15, the developing maxillary molar tissue is at the bud stage; at E17, it is at the cap stage; at E21, it is at the early bell stage; PN3 to PN5 comprises the advanced bell stage; at PN10, it is at the crown stage; at PN21, it is at the functional stage. Therefore, unlike the other major salivary glands, the development of mouse parotid salivary gland is completed through a process of prenatal and postnatal morphogenesis and becomes functional at about the same time as the developing tooth. The developmental completion times of the parotid salivary gland and tooth are closely related to the weaning time of animal.