Structural Analysis of Par-4 and Crystallographic Analysis of the Regulatory Domain

2022 ◽  
pp. 127-150
Author(s):  
J. Labahn ◽  
U. K. Tiruttani Subhramanyam
Keyword(s):  
Structural Analysis ◽  
Crystallographic Analysis ◽  
Regulatory Domain

scholarly journals X-ray structure of an unusual glycoluril derivative conformation: Structural analysis and influencing factors

2020 ◽  
pp. 174751982096101
Author(s):  
Jungang Wang ◽  
Shanghui Yang ◽  
Qiling Zou ◽  
Huanjiang Wang ◽  
Hongqing Li
Keyword(s):  
Hydrogen Bonding ◽  
Structural Analysis ◽  
Influencing Factors ◽  
Crystallographic Analysis ◽  
Solvation Effect ◽  
Conformational Behavior ◽  
Slow Evaporation ◽  
X Ray ◽  
Effect Of Solvent ◽  
Solvent Water

The synthesis and X-ray structure of a novel glycoluril derivative are described. The crystal of the glycoluril derivative is obtained by slow evaporation in a refrigerator at about 5 °C. X-ray crystallographic analysis revealed that the compound crystallized in an unusual as conformation instead of the usual clip-shaped aa conformation. Structural analysis shows that the solvation effect, hydrogen bonding, and space-occupying effect influenced the crystallization conformation of the derivative. The X-ray crystallographic analysis in this work provides additional crystallographic evidence of the as conformation of the 3U glycoluril derivative and shows the effect of solvent water on the conformational behavior.

Crystallization and preliminary crystallographic analysis of major nitroreductase from Escherichia coli

1999 ◽  
Vol 55 (11) ◽  
pp. 1901-1902 ◽  
Author(s):  
Toshiro Kobori ◽  
Woo Cheol Lee ◽  
Takako Akagi ◽  
Hiroshi Sasaki ◽  
Shuhei Zenno ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Polyethylene Glycol ◽  
Structural Analysis ◽  
Crystallographic Analysis ◽  
Diffusion Method ◽  
X Rays ◽  
Asymmetric Unit ◽  
Triclinic Space Group ◽  
Cell Dimensions ◽  
Polyethylene Glycol 6000

NADPH:nitrocompound oxidoreductase from Escherichia coli, NfsA, has been crystallized in the presence of FMN by the vapor-diffusion method using polyethylene glycol 6000 as a precipitant. The crystals belonged to the triclinic space group P1 with cell dimensions, a = 52.2, b = 52.7, c = 53.3 Å, \alpha = 75.1, β = 60.1, \gamma = 60.5°. The crystals are expected to contain two NfsA molecules per asymmetric unit. The crystals diffracted X-rays to at least 2.3 Å resolution and are appropriate for structural analysis at high resolution.

scholarly journals Structural analysis of a 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase with an N-terminal chorismate mutase-like regulatory domain

2012 ◽  
Vol 21 (6) ◽  
pp. 887-895 ◽  
Author(s):  
Samuel H. Light ◽  
Andrei S. Halavaty ◽  
George Minasov ◽  
Ludmilla Shuvalova ◽  
Wayne F. Anderson
Keyword(s):  
Structural Analysis ◽  
Chorismate Mutase ◽  
Regulatory Domain ◽  
Phosphate Synthase

scholarly journals A structural analysis of the regulatory domain from the cGMP-dependent protein kinase Iα

2011 ◽  
Vol 11 (S1) ◽  
Author(s):  
Brent W Osborne ◽  
Andrew T Menke ◽  
Donald K Blumenthal ◽  
Wolfgang R Dostmann
Keyword(s):  
Structural Analysis ◽  
Protein Kinase ◽  
Regulatory Domain ◽  
Dependent Protein Kinase ◽  
Cgmp Dependent Protein Kinase ◽  
Dependent Protein

scholarly journals Structural Clues to Rab GTPase Functional Diversity

2005 ◽  
Vol 280 (16) ◽  
pp. 15485-15488 ◽  
Author(s):  
Suzanne R. Pfeffer
Keyword(s):  
Structural Analysis ◽  
Functional Diversity ◽  
Membrane Trafficking ◽  
Crystallographic Analysis ◽  
Protein Family ◽  
Rab Gtpase ◽  
Rab Gtpases ◽  
Important Protein ◽  
Partner Proteins ◽  
Insight Into

Rab GTPases are key regulators of membrane trafficking in eukaryotes. Recent structural analysis of a number of Rabs, either alone or in complex with partner proteins, has provided new insight into the importance of both conserved and non-conserved features of these proteins that specify their unique functions and localizations. This review will highlight what we have learned from crystallographic analysis of this important protein family.

Current pivotal strategies leading a difficult target protein to a sample suitable for crystallographic analysis

2020 ◽  
Vol 48 (4) ◽  
pp. 1661-1673
Author(s):  
Atsuko Yamashita
Keyword(s):  
Electron Microscopy ◽  
Protein Structure ◽  
Structural Analysis ◽  
Sample Preparation ◽  
Protein Crystallization ◽  
Crystallographic Analysis ◽  
Expression And Purification ◽  
Cryo Electron Microscopy ◽  
Crystallization Conditions

Crystallographic structural analysis is an essential method for the determination of protein structure. However, crystallization of a protein of interest is the most difficult process in the analysis. The process is often hampered during the sample preparation, including expression and purification. Even after a sample has been purified, not all candidate proteins crystallize. In this mini-review, the current methodologies used to overcome obstacles encountered during protein crystallization are sorted. Specifically, the strategy for an effective crystallization is compared with a pipeline where various expression hosts and constructs, purification and crystallization conditions, and crystallization chaperones as target-specific binder proteins are assessed by a precrystallization screening. These methodologies are also developed continuously to improve the process. The described methods are useful for sample preparation in crystallographic analysis and other structure determination techniques, such as cryo-electron microscopy.

scholarly journals Micro-flow synthesis and structural analysis of sterically crowded diimine ligands with five aryl rings

2013 ◽  
Vol 9 ◽  
pp. 2336-2343 ◽  
Author(s):  
Shinichiro Fuse ◽  
Nobutake Tanabe ◽  
Akio Tannna ◽  
Yohei Konishi ◽  
Takashi Takahashi
Keyword(s):  
Structural Analysis ◽  
Nickel Complexes ◽  
Crystallographic Analysis ◽  
Detailed Structure ◽  
Flow Synthesis ◽  
X Ray ◽  
Diimine Ligands ◽  
One Step ◽  
Micro Flow ◽  
Polar Monomers

Sterically crowded diimine ligands with five aryl rings were prepared in one step in good yields using a micro-flow technique. X-ray crystallographic analysis revealed the detailed structure of the bulky ligands. The nickel complexes prepared from the ligands exerted high polymerization activity in the ethylene homopolymerization and copolymerization of ethylene with polar monomers.

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