Determination of the Three-Dimensional Structure of a New Crystalline Form ofN-Acetyl-Pro-Gly-Phe As Revealed by13C REDOR, X-Ray Diffraction, and Molecular Dynamics Calculation

1996 ◽  
Vol 100 (36) ◽  
pp. 14995-15004 ◽  
Author(s):  
Akira Naito ◽  
Katsuyuki Nishimura ◽  
Shigeki Kimura ◽  
Satoru Tuzi ◽  
Misako Aida ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Three Dimensional ◽  
Crystalline Form ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
X Ray ◽  
Three Dimensional Structure ◽  
Dynamics Calculation

scholarly journals Determination of the Three-dimensional Structure of Dislocations by Synchrotron White X-ray Topography Combined with a Topo-tomographic Technique

Materia Japan ◽  
2007 ◽  
Vol 46 (12) ◽  
pp. 823-823
Author(s):  
Seiji Kawado ◽  
Toshinori Taishi ◽  
Satoshi Iida ◽  
Yoshifumi Suzuki ◽  
Yoshinori Chikaura ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Dimensional Structure ◽  
X Ray ◽  
Three Dimensional Structure ◽  
Tomographic Technique

scholarly journals Three-dimensional structure of CdX (X=Se,Te) nanocrystals by total x-ray diffraction

2007 ◽  
Vol 102 (4) ◽  
pp. 044304 ◽  
Author(s):  
S. K. Pradhan ◽  
Z. T. Deng ◽  
F. Tang ◽  
C. Wang ◽  
Y. Ren ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
X Ray ◽  
Three Dimensional Structure

scholarly journals X-Ray Diffraction of Magnetically Oriented Microcrystals of Protein

2014 ◽  
Vol 70 (a1) ◽  
pp. C349-C349
Author(s):  
Shu Tsukui ◽  
Fumiko Kimura ◽  
Kimihiko Mizutani ◽  
Bunzo Mikami ◽  
Tsunehisa Kimura
Keyword(s):  
Single Crystal ◽  
Three Dimensional ◽  
Water Soluble ◽  
Dimensional Structure ◽  
Diffraction Measurement ◽  
X Ray Diffraction ◽  
Consolidation Process ◽  
X Ray ◽  
Three Dimensional Structure

Elucidation of the three-dimensional structure of biomolecules is of great importance because the three-dimensional structure is closely related to biological functions. X-ray single-crystal analysis is powerful method to analyze the structure, but it is sometimes difficult to grow a crystal sufficiently large for conventional or even synchrotron single-crystal X-ray measurement. We recently reported on a magnetically oriented microcrystal array (MOMA) [1] that is a composite in which microcrystals are aligned three-dimensionally in polymer matrix. Microcrystals are suspended in an ultraviolet-curable monomer and rotated non-uniformly in a static magnetic field to achieve three dimensional crystal alignment. Then, the monomer is photopolymerized to maintain the achieved alignment. We have successfully demonstrated that X-ray single crystal structure determinations through MOMA are possible for low molecular weight compounds [2] as well as protein. [3] However, the method with MOMA has two drawbacks: (i) the sample microcrystals cannot be recovered from a MOMA, which is especially serious problem in case of proteins, and (ii) the alignment is deteriorated during the consolidation process, causing low resolution. In this study, we attempt to solve these problems. First, we use a water-soluble sol as microcrystalline media and consolidate the alignment by gelation, which makes the recovery of microcrystals possible. Second, a magnetically oriented microcrystal suspension (MOMS) is used for in-situ X-ray diffraction measurement, which makes the sample recovery possible and enhances the resolution. We use lysozyme as a model protein for both cases. The in-situ method with in-house X-ray diffractometer gave diffraction spots about 3.0 Å resolutions. We plan to perform the same experiment at SPring-8.

scholarly journals History of protein crystallography in China

2007 ◽  
Vol 362 (1482) ◽  
pp. 1035-1042 ◽  
Author(s):  
Zihe Rao
Keyword(s):  
Protein Crystallography ◽  
Three Dimensional ◽  
Porcine Insulin ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
X Ray ◽  
X Ray Crystallography ◽  
Subsequent Determination ◽  
History Of

China has a strong background in X-ray crystallography dating back to the 1920s. Protein crystallography research in China was first developed following the successful synthesis of insulin in China in 1966. The subsequent determination of the three-dimensional structure of porcine insulin made China one of the few countries which could determine macromolecular structures by X-ray diffraction methods in the late 1960s and early 1970s. After a slow period during the 1970s and 1980s, protein crystallography in China has reached a new climax with a number of outstanding accomplishments. Here, I review the history and progress of protein crystallography in China and detail some of the recent research highlights, including the crystal structures of two membrane proteins as well as the structural genomics initiative in China.

Determination of the three-dimensional structure of dislocations in silicon by synchrotron white X-ray topography combined with a topo-tomographic technique

2004 ◽  
Vol 11 (4) ◽  
pp. 304-308 ◽  
Author(s):  
Seiji Kawado ◽  
Toshinori Taishi ◽  
Satoshi Iida ◽  
Yoshifumi Suzuki ◽  
Yoshinori Chikaura ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Dimensional Structure ◽  
X Ray ◽  
Three Dimensional Structure ◽  
Tomographic Technique

The biological crystallography without crystals

2017 ◽  
Vol 12 (1) ◽  
pp. 55-72 ◽  
Author(s):  
В.Ю. Лунин ◽  
V.Y. Lunin
Keyword(s):  
Three Dimensional ◽  
Scattering Data ◽  
Dimensional Structure ◽  
Biological Macromolecules ◽  
X Ray Diffraction ◽  
X Ray ◽  
Biological Objects ◽  
Standard Problem ◽  
Problems And Solutions

The main obstacle to the determination of the atomic structure of a biological macromolecule by X-ray structural analysis is the need to obtain a crystal of the object under study. This need is due to the complexity of the experimental registration of scattering from a separate molecule. However, it is not always possible to get crystals of biological objects. The development of experimental techniques, in particular the emergence of the X-ray free-electron lasers, allows to approach the practical solution of the problem of registration of the scattering from an isolated particle and thereby to obtain information about the three-dimensional structure of non-crystalline biological objects by X-ray diffraction methods. Sampling of experimental scattering data makes the task of the structure determination of a single particle equivalent to the standard problem of biological crystallography, which allows to extend the biological crystallography techniques to the study of isolated biological particles (individual cells, organelles, molecular machines and, in the future, biological macromolecules). This article is devoted to the state of the art in this area, problems and solutions.

A multiple-common-lines method to determine the orientation of snapshot diffraction patterns from single particles

2014 ◽  
Vol 70 (4) ◽  
pp. 364-372 ◽  
Author(s):  
Liang Zhou ◽  
Tian-Yi Zhang ◽  
Zhong-Chuan Liu ◽  
Peng Liu ◽  
Yu-Hui Dong
Keyword(s):  
Three Dimensional ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
Single Particles ◽  
X Ray ◽  
Three Dimensional Structure ◽  
Individual Object ◽  
Common Lines ◽  
Diffraction Imaging ◽  
Diffraction Patterns

With the development of X-ray free-electron lasers (XFELs), it is possible to determine the three-dimensional structures of noncrystalline objects with coherent X-ray diffraction imaging. In this diffract-and-destroy mode, many snapshot diffraction patterns are obtained from the identical objects which are presented one by one in random orientations to the XFEL beam. Determination of the orientation of an individual object is essential for reconstruction of a three-dimensional structure. Here a new method, called the multiple-common-lines method, has been proposed to determine the orientations of high- and low-signal snapshot diffraction patterns. The mean errors of recovered orientations (α, β, γ) of high- and low-signal patterns are about 0.14, 0.06, 0.12 and 0.77, 0.31, 0.60°, respectively; both sets of errors can meet the requirements of the reconstruction of a three-dimensional structure.

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