Addition of twisted 1,1-bis(thioacyl)-2,2-diaminoethylenes to dimethyl acetylenedicarboxylate. 2. Structure determination of two isomeric spiro adducts by x-ray crystallography and of a rearrangement product by the 2D INADEQUATE technique

1991 ◽  
Vol 56 (16) ◽  
pp. 4919-4925 ◽  
Author(s):  
Agha Zul Qarnain Khan ◽  
Jan Sandstroem ◽  
Karl Eric Bergquist ◽  
Chih Yi Cheng ◽  
Sue Lein Wang
Keyword(s):  
Structure Determination ◽  
Dimethyl Acetylenedicarboxylate ◽  
Rearrangement Product ◽  
X Ray ◽  
X Ray Crystallography

scholarly journals Structure determination of GPCRs: cryo-EM compared with X-ray crystallography

2021 ◽  
Author(s):  
Javier García-Nafría ◽  
Christopher G. Tate
Keyword(s):  
Structural Biology ◽  
Structure Determination ◽  
Drug Targets ◽  
Cellular Systems ◽  
Single Family ◽  
Structure Based Drug Design ◽  
X Ray ◽  
Surface Receptors ◽  
X Ray Crystallography

G protein-coupled receptors (GPCRs) are the largest single family of cell surface receptors encoded by the human genome and they play pivotal roles in co-ordinating cellular systems throughout the human body, making them ideal drug targets. Structural biology has played a key role in defining how receptors are activated and signal through G proteins and β-arrestins. The application of structure-based drug design (SBDD) is now yielding novel compounds targeting GPCRs. There is thus significant interest from both academia and the pharmaceutical industry in the structural biology of GPCRs as currently only about one quarter of human non-odorant receptors have had their structure determined. Initially, all the structures were determined by X-ray crystallography, but recent advances in electron cryo-microscopy (cryo-EM) now make GPCRs tractable targets for single-particle cryo-EM with comparable resolution to X-ray crystallography. So far this year, 78% of the 99 GPCR structures deposited in the PDB (Jan–Jul 2021) were determined by cryo-EM. Cryo-EM has also opened up new possibilities in GPCR structural biology, such as determining structures of GPCRs embedded in a lipid nanodisc and multiple GPCR conformations from a single preparation. However, X-ray crystallography still has a number of advantages, particularly in the speed of determining many structures of the same receptor bound to different ligands, an essential prerequisite for effective SBDD. We will discuss the relative merits of cryo-EM and X-ray crystallography for the structure determination of GPCRs and the future potential of both techniques.

scholarly journals Structure Determination of Membrane Proteins Using X-Ray Crystallography

2021 ◽  
pp. 101-136
Author(s):  
Evan Billings ◽  
Karl Lundquist ◽  
Claire Overly ◽  
Karthik Srinivasan ◽  
Nicholas Noinaj
Keyword(s):  
Membrane Proteins ◽  
Structure Determination ◽  
X Ray ◽  
X Ray Crystallography

The structure determination of a new cembranolide diterpene from the soft coral Lobophytum cristigalli (Coelenterata, Octocorallia, Alcyonacea)

1984 ◽  
Vol 37 (3) ◽  
pp. 545 ◽  
Author(s):  
BF Bowden ◽  
JC Coll ◽  
MSL de Costa ◽  
MF Mackay ◽  
M Mahendran ◽  
...  
Keyword(s):  
Sri Lanka ◽  
Structure Determination ◽  
Soft Coral ◽  
X Ray ◽  
X Ray Crystallography

A specimen of Lobophytum cristigalli collected in Sri Lanka afforded two cembranolide diterpenes (7E,11E,1R,2S,3R,4R,14S)-14-acetoxy-3,4-epoxycembra-7,11,15-trien-17,2-olide (6)* and the corresponding alcohol (7). Their structures were deduced spectroscopically and detailed stereochemistry of (6) was determined by X-ray crystallography.

scholarly journals Structure determination of a human virus by the combination of cryo-EM and X-ray crystallography

2016 ◽  
Vol 2 (2-4) ◽  
pp. 55-68 ◽  
Author(s):  
Zheng Liu ◽  
Tom S. Y. Guu ◽  
Jianhao Cao ◽  
Yinyin Li ◽  
Lingpeng Cheng ◽  
...  
Keyword(s):  
Structure Determination ◽  
Human Virus ◽  
X Ray ◽  
X Ray Crystallography
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