scholarly journals Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience

2017 ◽  
Vol 13 ◽  
pp. 1145-1167 ◽  
Author(s):  
Serge Pérez ◽  
Daniele de Sanctis
Keyword(s):  
Synchrotron Radiation ◽  
Structural Characterization ◽  
Crystalline State ◽  
Structural Diversity ◽  
Interacting Proteins ◽  
X Ray ◽  
Wide Range ◽  
Kinetics Of

Synchrotron radiation is the most versatile way to explore biological materials in different states: monocrystalline, polycrystalline, solution, colloids and multiscale architectures. Steady improvements in instrumentation have made synchrotrons the most flexible intense X-ray source. The wide range of applications of synchrotron radiation is commensurate with the structural diversity and complexity of the molecules and macromolecules that form the collection of substrates investigated by glycoscience. The present review illustrates how synchrotron-based experiments have contributed to our understanding in the field of structural glycobiology. Structural characterization of protein–carbohydrate interactions of the families of most glycan-interacting proteins (including glycosyl transferases and hydrolases, lectins, antibodies and GAG-binding proteins) are presented. Examples concerned with glycolipids and colloids are also covered as well as some dealing with the structures and multiscale architectures of polysaccharides. Insights into the kinetics of catalytic events observed in the crystalline state are also presented as well as some aspects of structure determination of protein in solution.

Kinetics of lysozyme refolding: structural characterization of a non-specifically collapsed state using time-resolved X-ray scattering

1998 ◽  
Vol 276 (1) ◽  
pp. 225-237 ◽  
Author(s):  
Lingling Chen ◽  
Gudrun Wildegger ◽  
Thomas Kiefhaber ◽  
Keith O Hodgson ◽  
Sebastian Doniach
Keyword(s):  
Structural Characterization ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Lysozyme Refolding ◽  
Kinetics Of ◽  
Ray Scattering

scholarly journals Kinetic and Structural Characterization of the First B3 Metallo-β-Lactamase with an Active Site Glutamic Acid

2021 ◽  
Author(s):  
Liam A. Wilson ◽  
Esmée G. Knaven ◽  
Marc T. Morris ◽  
Marcelo Monteiro Pedroso ◽  
Christopher J. Schofield ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Structural Characterization ◽  
Active Site ◽  
Structural Diversity ◽  
Kinetic Properties ◽  
Design Studies ◽  
Degrading Bacterium ◽  
Active Site Motif ◽  
Wide Range

The structural diversity in metallo-β-lactamases (MBLs), especially in the vicinity of the active site, has been a major hurdle in the development of clinically effective inhibitors. Representatives from three variants of the B3 MBL subclass, containing either the canonical HHH/DHH active site motif (present in the majority of MBLs in this subclass) or the QHH/DHH (B3-Q) or HRH/DQK (B3-RQK) variations were reported previously. Here, we describe the structure and kinetic properties of the first example (SIE-1) of a fourth variant containing the EHH/DHH active site motif (B3-E). SIE-1 was identified in the hexachlorocyclohexane-degrading bacterium Sphingobium indicum , and kinetic analyses demonstrate that although it is active against a wide range of antibiotics its efficiency is lower than that of other B3 MBLs, but with improved efficiency towards cephalosporins relative to other β-lactam substrates. The overall fold of SIE-1 is characteristic of the MBLs; the notable variation is observed in the Zn1 site due to the replacement of the canonical His116 by a glutamate. The unusual preference of SIE-1 for cephalosporins and its occurrence in a widespread environmental organism suggests scope for increased MBL-mediated β-lactam resistance. It is thus relevant to include SIE-1 into MBL inhibitor design studies to widen the therapeutic scope of much needed anti-resistance drugs.

Single Crystal X-Ray Structural Characterization of [BiX2(S2CNEt2)]Infinity∞, X=Cl, Br

1994 ◽  
Vol 47 (2) ◽  
pp. 405 ◽  
Author(s):  
PK Bharadwaj ◽  
AM Lee ◽  
BW Skelton ◽  
BR Srinivasan ◽  
AH White
Keyword(s):  
Single Crystal ◽  
Sulfur Atom ◽  
Structural Characterization ◽  
Structure Determination ◽  
Room Temperature ◽  
X Ray ◽  
Structure Determinations

Single-crystal room-temperature X-ray structure determinations of the title compounds have been carried out. The two compounds are isomorphous, and isomorphous with the previously determined iodide analogue, being monoclinic, P 21/c, a ≈ 10.0, b ≈ 14.9, c ≈ 7.8 Ǻ, β ≈ 92°, Z = 4 formula units; residuals were 0.037, 0.036 for 2197, 1654 'observed' reflections for X = Cl , Br respectively. As in the iodide, the complexes are infinite polymers, with successive bismuth atoms bridged by the two halides and one sulfur atom of the ligand , which also chelates each bismuth. The structure determination of C5H5NCONEt2]2 [Cl5Bi(NC5H5)], isostructural with its thiocarbamoyl analogue, is also recorded.

Lewis-Base Adducts of Lead(II) Compounds. III. Synthesis and Structural Characterization of Mononuclear (Nitrato-O,O′)bis(1,10-phenanthroline)-(thiocyanato-N)lead(II)

1989 ◽  
Vol 42 (2) ◽  
pp. 335 ◽  
Author(s):  
LM Engelhardt ◽  
JM Patrick ◽  
AH White
Keyword(s):  
Single Crystal ◽  
Structural Characterization ◽  
Structure Determination ◽  
Title Compound ◽  
Lone Pair ◽  
Lewis Base ◽  
Lead Atom ◽  
X Ray

The isolation and single-crystal X-ray structure determination of the title compound, [(phen)2Pb(NCS)(O2NO)] is described; crystals are triclinic, P1, a 15.554(7), b 9-670(4), c 8.429(3) α 72.53(3), β 81.90(3), γ 72.88(3)� Z = 2, yielding R 0.052 for 3405 independent 'observed' reflections. The lead atom is seven-coordinate [Pb-N 2.49(1)-2.60(1) (phen), 2.89(1) (NCS); Pb-O 2.75(1), 2.89(1) �] with a large vacancy in the coordination sphere, possibly indicative of a stereochemically active lone pair.

The crystalline-state photochromism, thermochromism and X-ray structural characterization of a new spiroxazine

2003 ◽  
Vol 57 (2) ◽  
pp. 149-159 ◽  
Author(s):  
Hee-Jung Suh ◽  
Woo-Taik Lim ◽  
Jian-Zhong Cui ◽  
Heung-Soo Lee ◽  
Ghyung-Hwa Kim ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Crystalline State ◽  
X Ray

Structural characterization of ultrathin cuprate artificial superconducting structures by x-ray synchrotron radiation

2003 ◽  
Vol 94 (10) ◽  
pp. 6991-6993 ◽  
Author(s):  
C. Aruta ◽  
M. Angeloni ◽  
G. Balestrino ◽  
P. G. Medaglia ◽  
P. Orgiani ◽  
...  
Keyword(s):  
Synchrotron Radiation ◽  
Structural Characterization ◽  
X Ray

Structural Characterization of Nickel(II) Tetraphenylporphyrin

1996 ◽  
Vol 49 (12) ◽  
pp. 1273 ◽  
Author(s):  
AL Maclean ◽  
GJ Foran ◽  
BJ Kennedy ◽  
P Turner ◽  
TW Hambley
Keyword(s):  
Synchrotron Radiation ◽  
Single Crystal ◽  
Bond Length ◽  
Diffraction Pattern ◽  
Structural Characterization ◽  
X Ray Diffraction ◽  
X Ray ◽  
Bond Lengths ◽  
Single Crystal Analysis

The structure of 5,10,15,20-tetraphenylporphinatonickel(II) ([Ni( tpp )]) has been studied by both X-ray diffraction (powder and single-crystal methods) and EXAFS. The bond lengths obtained from analysis of the EXAFS agree, within standard deviations, with those obtained from the X-ray diffraction studies. The Ni-N bond length of 1.93(1) Ǻ agrees especially well with the value of 1.931(2) Ǻ obtained from the single-crystal analysis. The powder X-ray diffraction pattern, collected by using synchrotron radiation, is presented.

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