scholarly journals The Practical Aspect of Structure Analysis of Protein Crystal

1968 ◽  
Vol 8 (1) ◽  
pp. 1-10
Author(s):  
Tunehiro TAKANO
Keyword(s):  
Structure Analysis ◽  
Practical Aspect ◽  
Protein Crystal

scholarly journals Microfluidic Approaches for Protein Crystal Structure Analysis

2016 ◽  
Vol 32 (1) ◽  
pp. 3-9 ◽  
Author(s):  
Masatoshi MAEKI ◽  
Hiroshi YAMAGUCHI ◽  
Manabu TOKESHI ◽  
Masaya MIYAZAKI
Keyword(s):  
Crystal Structure ◽  
Structure Analysis ◽  
Crystal Structure Analysis ◽  
Protein Crystal ◽  
Protein Crystal Structure

scholarly journals Structure analysis of protein crystal

1967 ◽  
Vol 7 (6) ◽  
pp. 313-323
Author(s):  
Tamaichi ASHIDA
Keyword(s):  
Structure Analysis ◽  
Protein Crystal

scholarly journals Room-temperature crystallography using a microfluidic protein crystal array device and its application to protein–ligand complex structure analysis

2020 ◽  
Vol 11 (34) ◽  
pp. 9072-9087
Author(s):  
Masatoshi Maeki ◽  
Sho Ito ◽  
Reo Takeda ◽  
Go Ueno ◽  
Akihiko Ishida ◽  
...  
Keyword(s):  
Structure Analysis ◽  
Room Temperature ◽  
Complex Structure ◽  
Protein Crystallography ◽  
Protein Crystal ◽  
Ligand Complex

Room temperature protein crystallography and its application to protein–ligand complex structure analysis was demonstrated using a microfluidic protein crystal array device.

200kv superconducting cryo electron microscope

1987 ◽  
Vol 45 ◽  
pp. 642-643
Author(s):  
M. Iwatsuki ◽  
Y. Kokubo ◽  
Y. Harada ◽  
J. Lehman
Keyword(s):  
Electron Microscope ◽  
Structure Analysis ◽  
Organic Materials ◽  
Strong Interactions ◽  
Specimen Preparation ◽  
Great Effort ◽  
Electron Microscopic ◽  
Crystal Fields ◽  
Special Skill ◽  
Long Time

In recent years, the electron microscope has been significantly improved in resolution and we can obtain routinely atomic-level high resolution images without any special skill. With this improvement, the structure analysis of organic materials has become one of the interesting targets in the biological and polymer crystal fields.Up to now, X-ray structure analysis has been mainly used for such materials. With this method, however, great effort and a long time are required for specimen preparation because of the need for larger crystals. This method can analyze average crystal structure but is insufficient for interpreting it on the atomic or molecular level. The electron microscopic method for organic materials has not only the advantage of specimen preparation but also the capability of providing various information from extremely small specimen regions, using strong interactions between electrons and the substance. On the other hand, however, this strong interaction has a big disadvantage in high radiation damage.

Spot-scan imaging of ice-embedded catalase crystal on a slow-scan CCD camera in a 400-kV electron cryomicroscope

1994 ◽  
Vol 52 ◽  
pp. 98-99
Author(s):  
Wah Chiu ◽  
Michael Sherman ◽  
Jaap Brink
Keyword(s):  
Electron Diffraction ◽  
Ccd Camera ◽  
Protein Crystal ◽  
Modulation Transfer ◽  
Measured Intensity ◽  
3 Dimensional ◽  
Dimensional Reconstruction ◽  
Diffraction Patterns ◽  
Complex Crystal

In protein electron crystallography, both low dose electron diffraction patterns and images are needed to provide accurate amplitudes and phases respectively for a 3-dimensional reconstruction. We have demonstrated that the Gatan 1024x1024 model 679 slow-scan CCD camera is useful to record electron diffraction intensities of glucose-embedded crotoxin complex crystal to 3 Å resolution. The quality of the electron diffraction intensities is high on the basis of the measured intensity equivalence ofthe Friedel-related reflections. Moreover, the number of patterns recorded from a single crystal can be as high as 120 under the constraints of radiation damage and electron statistics for the reflections in each pattern.A limitation of the slow-scan CCD camera for recording electron images of protein crystal arises from the relatively large pixel size, i.e. 24 μm (provided by Gatan). The modulation transfer function of our camera with a P43 scintillator has been determined for 400 keV electrons and shows an amplitude fall-off to 0.25 at 1/60 μm−1.

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