Studies on the action of X-rays on aqueous solutions of nucleic acids and some nucleotides

1955 ◽  
Vol 11 (6) ◽  
pp. 219-221 ◽  
Author(s):  
M. Daniels ◽  
G. Scholes ◽  
J. Weiss
Keyword(s):  
Nucleic Acids ◽  
Aqueous Solutions ◽  
X Rays

New Possibilities of Investigating Nucleic Acids and Nucleoproteins in Aqueous Solutions by Infrared Spectroscopy

Nature ◽  
1972 ◽  
Vol 235 (5338) ◽  
pp. 386-388 ◽  
Author(s):  
M. SHIE ◽  
I. G. KHARITONENKOV ◽  
T. I. TIKHONENKO ◽  
Yu. N. CHIRGADZE
Keyword(s):  
Infrared Spectroscopy ◽  
Nucleic Acids ◽  
Aqueous Solutions

‘After-effect’ in Aqueous Solutions of Deoxyribonucleic Acid irradiated with X-Rays

Nature ◽  
1953 ◽  
Vol 171 (4365) ◽  
pp. 1153-1154 ◽  
Author(s):  
MALCOLM DANIELS ◽  
GEORGE SCHOLES ◽  
JOSEPH WEISS
Keyword(s):  
Aqueous Solutions ◽  
Deoxyribonucleic Acid ◽  
X Rays ◽  
After Effect

A solution-free crystal-mounting platform for native SAD

2020 ◽  
Vol 76 (10) ◽  
pp. 938-945
Author(s):  
Jian Yu ◽  
Akira Shinoda ◽  
Koji Kato ◽  
Isao Tanaka ◽  
Min Yao
Keyword(s):  
Data Collection ◽  
Nucleic Acids ◽  
Protein Structures ◽  
Anomalous Scattering ◽  
X Rays ◽  
Long Wavelength ◽  
Light Atoms ◽  
Sad Phasing ◽  
Anomalous Signal

The native SAD phasing method uses the anomalous scattering signals from the S atoms contained in most proteins, the P atoms in nucleic acids or other light atoms derived from the solution used for crystallization. These signals are very weak and careful data collection is required, which makes this method very difficult. One way to enhance the anomalous signal is to use long-wavelength X-rays; however, these wavelengths are more strongly absorbed by the materials in the pathway. Therefore, a crystal-mounting platform for native SAD data collection that removes solution around the crystals has been developed. This platform includes a novel solution-free mounting tool and an automatic robot, which extracts the surrounding solution, flash-cools the crystal and inserts the loop into a UniPuck cassette for use in the synchrotron. Eight protein structures (including two new structures) have been successfully solved by the native SAD method from crystals prepared using this platform.

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