Improvements in electron microscopy by application of superconductivity

Dietrich, I.; Fox, F.; Knapek, E.; Lefranc, G.; Nachtrieb, K.; Weyl, R.; Zerbst, H.

doi:10.1016/s0304-3991(76)91487-x

Cited by 85 publications

(11 citation statements)

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“…In the Glaeser lab, Steve Hayward built a stage based on the JEOL design (Hayward and Glaeser, 1980) that was capable of routinely achieving this resolution, but it could only maintain a temperature of −90°C, suitable for work with glucose embedded purple membrane. Specialty microscopes, such as one in Germany that was equipped with a superconducting objective lens system (Dietrich et al, 1977), could also routinely obtain high resolution images of purple membrane. Both of these instruments contributed to the first high resolution purple membrane structure (Henderson et al, 1990).…”

Section: Other Technologies Important For the Current Status Of Cryoemmentioning

confidence: 99%

Retrospective on the early development of cryoelectron microscopy of macromolecules and a prospective on opportunities for the future

Taylor

Glaeser

2008

Journal of Structural Biology

156

119

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Methods for preserving specimen hydration in protein crystals were pursued in the early 1970s as a prerequisite for protein crystallography using an electron microscope. Three laboratories approached this question from very different directions. One built a differentially pumped hydration chamber that could maintain the crystal in a liquid water environment, a second maintained hydration by rapidly freezing the protein crystal and examining it in a cold stage, and the third replaced the water of hydration by using glucose in the same way as one had previously used "negative stains". Each of these early efforts succeeded in preserving the structures of protein crystals at high resolution within the vacuum of the electron microscope, as demonstrated by electron diffraction patterns. The next breakthrough came in the early 1980s when a technique was devised to preserve noncrystalline specimens by freezing them within vitreous ice. Since then, with the development of high stability cold stages and transfer mechanisms compatible with many instrument platforms, and by using commercially provided low-dose imaging techniques to avoid radiation damage, there has been an explosion of applications. These now include single particles, helical filaments, 2-D arrays and even whole cells, where the most exciting recent applications involve cryoelectron tomography. These achievements and possibilities generate a new set of research opportunities associated with increasing the reliability and throughput with which specimens can be studied by cryoEM.

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Section: Other Technologies Important For the Current Status Of Cryoemmentioning

confidence: 99%

Retrospective on the early development of cryoelectron microscopy of macromolecules and a prospective on opportunities for the future

Taylor

Glaeser

2008

Journal of Structural Biology

156

119

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“…But one can certainly experiment along these lines, since it is now possible to build high-resolution cryomicroscopes (cf. [231).…”

Section: Discussionmentioning

confidence: 99%

Electron Diffraction with the Transmission Electron Microscope as a Phase‐Determining Diffractometer—From Spatial Frequency Filtering to the Three‐Dimensional Structure Analysis of Ribosomes

Hoppe

1983

Angew. Chem. Int. Ed. Engl.

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Dedicated to Professor Adolf Butenandt on the occasion of his 80th birthdayChemists recognize X-ray crystaI structure analysis and electron microscopy as powerful methods of analysis. In the last 20 years the basic ideas of X-ray diffraction analysis have been extended to the field of electron microscopy, whereby an image-forming apparatus is converted into an electron diffractometer, and through which an old dream of crystallographers can be realized-the measurement of the phase shift of scattered waves, a prerequisite for the direct calculation of structures. Its most important area of application, like that of the X-ray diffractometer, is in three-dimensional structure analysis-in all fields of science. However, beyond crystallography, aperiodic structures (comparable to crystals with a single unit cell) can also be analyzed three-dimensionally. In this progress report, the development of the first idea (spatial frequency filtering) to the analysis of ribosomal particles is outlined. Attention will be focused primarily on quantitative methods for the measurement of scattered rays, which are also usable beyond the conventional limit of resolution, down to atomic resolution. In the course of this work in 1968, the principle of the three-dimensional analysis of native biological crystal structures using the electron microscope, as worked with today in many laboratories, was developed. In Munich, however, further research focused on the three-dimensional analysis of aperiodic and individual (especially biological) objects. The analysis of 50s-subunits of the procaryotic ribosome of E. coli showed surprisingly good reproducibility of the results (although only within the same orientation), allowing the deduction of almost ideal average model structures from a limited number of particles.

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“…In the last years it has been possible to image very beam-sensitive crystals in a cryomicroscope with a resolution of 3.5 A ( Fig. 18; Zemlin et al, 1985; see also Dietrich et al, 1971;Henderson and Unwin, 1975). The specimens were cooled down to -269 °C.…”

Section: G Development Of Electron Microscopy After 1945mentioning

confidence: 99%

The development of the electron microscope and of electron microscopy

Руска

1987

Rev. Mod. Phys.

119

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A. PARENTS* HOUSE, FAMILYA month ago, the Nobel Foundation sent me its yearbook of 1985. From it I learned that many Nobel lectures are downright scientific lectures, interspersed with curves, synoptic tables, and quotations. I am somewhat reluctant to give here such a lecture on something that can be looked up in any modern schoolbook on physics. I will therefore not so much report here on physical and technical details and their connections but rather on the human experiences-some joyful events and many disappointments which were not spared me and my colleagues on our way to the final breakthrough. This is not meant to be a complaint though; I rather feel that such experiences of scientists in quest of new approaches are absolutely understandable, or even normal.In such a representation I must, of course, consider the influence of my environment, in particular of my family. There had already been some scientists in my family: My father, Julius Ruska, was a historian of sciences in Heidelberg and Berlin; my uncle, Max Wolf, astronomer in Heidelberg; his assistant, a former pupil of my father and my godfather, August Kopff, Director of the Institute for Astronomical Calculation of the former Friedrich-Wilhelm University in Berlin. A cousin of my mother, Alfred Hoche, was Professor for Psychiatry in Freiburg/Breisgau; my grandfather from my mother's side, Adalbert Merx, theologian in Giessen and Heidelberg.My parents lived in Heidelberg and had seven children. I was the fifth, my brother Helmut the sixth. To him I had particularly close and friendly relations as long as I can remember. Early, optical instruments made a strong impression on us. Several times Uncle Max had shown us the telescopes at the observatory on the Konigstuhl near Heidelberg headed by him. With the light microscope, as well, we soon had impressive, yet contradictory, relations. In the second floor of our house, my father had two study rooms connected by a broad sliding door, which usually was open. One room he used for his scientific historical studies relating to classical philology, the other for his scientific interests, in particular mineralogy, botany, and zoology. When our games with neighbors' kids in front This lecture was delivered 8 December 1986, on the occasion of the presentation of the 1986 Nobel Prize in Physics. of the house became too noisy, he would knock at the window panes. This usually having only a brief effect, he soon knocked a second time, this time considerably louder. At the third knock, Helmut and I had to come to his room and sit still on a low wooden stool, dos-d-dos, up to one hour at 2 m distance from his desk. While doing so we would see on a table in the other room the pretty yellowish wooden box that housed my father's big Zeiss microscope, which we were strictly forbidden to touch. He sometimes demonstrated to us interesting objects under the microscope, it is true; for good reasons, however, he feared that children's hands would damage the objective or the specimen by clumsy manipulation of the coarse and ...

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Improvements in electron microscopy by application of superconductivity

Cited by 85 publications

References 1 publication

Retrospective on the early development of cryoelectron microscopy of macromolecules and a prospective on opportunities for the future

Retrospective on the early development of cryoelectron microscopy of macromolecules and a prospective on opportunities for the future

Electron Diffraction with the Transmission Electron Microscope as a Phase‐Determining Diffractometer—From Spatial Frequency Filtering to the Three‐Dimensional Structure Analysis of Ribosomes

The development of the electron microscope and of electron microscopy

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