scholarly journals Determination of the X-ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography

2010 ◽  
Vol 19 (10) ◽  
pp. 1840-1849 ◽  
Author(s):  
James R. Banigan ◽  
Kalyaneswar Mandal ◽  
Michael R. Sawaya ◽  
Vilasak Thammavongsa ◽  
Antoni P. A. Hendrickx ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Snake Venom ◽  
Protein Crystallography ◽  
Venom Protein ◽  
X Ray

scholarly journals Fully Convergent Chemical Synthesis of Ester Insulin: Determination of the High Resolution X-ray Structure by Racemic Protein Crystallography

2013 ◽  
Vol 135 (8) ◽  
pp. 3173-3185 ◽  
Author(s):  
Michal Avital-Shmilovici ◽  
Kalyaneswar Mandal ◽  
Zachary P. Gates ◽  
Nelson B. Phillips ◽  
Michael A. Weiss ◽  
...  
Keyword(s):  
High Resolution ◽  
Chemical Synthesis ◽  
Protein Crystallography ◽  
X Ray

One-pot hydrazide-based native chemical ligation for efficient chemical synthesis and structure determination of toxin Mambalgin-1

2014 ◽  
Vol 50 (44) ◽  
pp. 5837-5839 ◽  
Author(s):  
Man Pan ◽  
Yao He ◽  
Ming Wen ◽  
Fangming Wu ◽  
Demeng Sun ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Snake Venom ◽  
Structure Determination ◽  
Native Chemical Ligation ◽  
One Pot ◽  
Chemical Ligation ◽  
Venom Toxin ◽  
Snake Venom Toxin ◽  
Switch Strategy

An efficient one-pot chemical synthesis of snake venom toxin Mambalgin-1 was achieved using an azide-switch strategy combined with hydrazide-based native chemical ligation.

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.

Protein crystallography using a multilayer monochromator

1998 ◽  
Vol 5 (3) ◽  
pp. 494-496 ◽  
Author(s):  
Ashley M. Deacon ◽  
Todd Appleby ◽  
Donald H. Bilderback ◽  
Steven E. Ealick ◽  
Ernest Fontes ◽  
...  
Keyword(s):  
Room Temperature ◽  
Protein Crystallography ◽  
High Energy ◽  
Short Exposure ◽  
Synchrotron Source ◽  
X Ray ◽  
Methylthioadenosine Phosphorylase ◽  
Data Processing Software ◽  
Wide Energy

A multilayer monochromator was installed on a bending-magnet beamline at the Cornell High Energy Synchrotron Source (CHESS) and was used to provide an unfocused pseudo-monochromatic X-ray beam for protein crystallography experiments. Datasets were collected from lysozyme at room temperature and human methylthioadenosine phosphorylase at 100 K. The wide energy bandpass of the multilayer allowed short exposure times, typically only a few times longer than on a focused multipole wiggler beamline. The diffraction images were processed using unmodified monochromatic data-processing software to yield datasets of good quality. These first measurements demonstrate that multilayer monochromators can be readily applied to the rapid structure determination of many typical-sized macromolecules.

Total chemical synthesis and X-ray structure of kaliotoxin by racemic protein crystallography

2010 ◽  
Vol 46 (43) ◽  
pp. 8174 ◽  
Author(s):  
Brad L. Pentelute ◽  
Kalyaneswar Mandal ◽  
Zachary P. Gates ◽  
Michael R. Sawaya ◽  
Todd O. Yeates ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Protein Crystallography ◽  
X Ray

scholarly journals Ab initiophasing of the diffraction of crystals with translational disorder

2019 ◽  
Vol 75 (1) ◽  
pp. 25-40 ◽  
Author(s):  
Andrew J. Morgan ◽  
Kartik Ayyer ◽  
Anton Barty ◽  
Joe P. J. Chen ◽  
Tomas Ekeberg ◽  
...  
Keyword(s):  
Protein Structure ◽  
Protein Structures ◽  
Protein Crystallography ◽  
Biological Molecules ◽  
Protein Crystal ◽  
Projection Algorithm ◽  
X Ray ◽  
Angular Extent ◽  
Crystal Lattice Site

To date X-ray protein crystallography is the most successful technique available for the determination of high-resolution 3D structures of biological molecules and their complexes. In X-ray protein crystallography the structure of a protein is refined against the set of observed Bragg reflections from a protein crystal. The resolution of the refined protein structure is limited by the highest angle at which Bragg reflections can be observed. In addition, the Bragg reflections alone are typically insufficient (by a factor of two) to determine the structureab initio, and so prior information is required. Crystals formed from an imperfect packing of the protein molecules may also exhibit continuous diffraction between and beyond these Bragg reflections. When this is due to random displacements of the molecules from each crystal lattice site, the continuous diffraction provides the necessary information to determine the protein structure without prior knowledge, to a resolution that is not limited by the angular extent of the observed Bragg reflections but instead by that of the diffraction as a whole. This article presents an iterative projection algorithm that simultaneously uses the continuous diffraction as well as the Bragg reflections for the determination of protein structures. The viability of this method is demonstrated on simulated crystal diffraction.

Lateral resolution of the electron microbeam analysis

1978 ◽  
Vol 36 (1) ◽  
pp. 542-543
Author(s):  
H.J. Dudek
Keyword(s):  
Quantitative Analysis ◽  
Depth Resolution ◽  
Lateral Resolution ◽  
Cylindrical Particle ◽  
Correction Procedure ◽  
X Ray ◽  
Element Concentrations ◽  
Microbeam Analysis ◽  
The Matrix

The chemical inhomogenities in modern materials such as fibers, phases and inclusions, often have diameters in the region of one micrometer. Using electron microbeam analysis for the determination of the element concentrations one has to know the smallest possible diameter of such regions for a given accuracy of the quantitative analysis.In th is paper the correction procedure for the quantitative electron microbeam analysis is extended to a spacial problem to determine the smallest possible measurements of a cylindrical particle P of high D (depth resolution) and diameter L (lateral resolution) embeded in a matrix M and which has to be analysed quantitative with the accuracy q. The mathematical accounts lead to the following form of the characteristic x-ray intens ity of the element i of a particle P embeded in the matrix M in relation to the intensity of a standard S

Sem and X-Ray Analysis of Renal and Biliary Calculi

1976 ◽  
Vol 34 ◽  
pp. 306-307
Author(s):  
R. J. Narconis ◽  
G. L. Johnson
Keyword(s):  
Chemical Constituents ◽  
Natural State ◽  
X Ray Diffraction ◽  
Chemical Methods ◽  
X Ray ◽  
Additional Dimension ◽  
Biliary Calculi ◽  
Calculus Formation ◽  
Scanning Electron

Analysis of the constituents of renal and biliary calculi may be of help in the management of patients with calculous disease. Several methods of analysis are available for identifying these constituents. Most common are chemical methods, optical crystallography, x-ray diffraction, and infrared spectroscopy. The application of a SEM with x-ray analysis capabilities should be considered as an additional alternative.A scanning electron microscope equipped with an x-ray “mapping” attachment offers an additional dimension in its ability to locate elemental constituents geographically, and thus, provide a clue in determination of possible metabolic etiology in calculus formation. The ability of this method to give an undisturbed view of adjacent layers of elements in their natural state is of advantage in determining the sequence of formation of subsequent layers of chemical constituents.

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