Combination of cross polarization/magic angle spinning NMR and x-ray crystallography: structure and dynamics in a low-symmetry molecular crystal, potassium penicillin V

1993 ◽  
Vol 115 (13) ◽  
pp. 5636-5650 ◽  
Author(s):  
Jamila Fattah ◽  
J. Mark Twyman ◽  
Stephen J. Heyes ◽  
David J. Watkin ◽  
Alison J. Edwards ◽  
...  
Keyword(s):  
Molecular Crystal ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Cross Polarization ◽  
X Ray ◽  
X Ray Crystallography ◽  
Structure And Dynamics ◽  
Potassium Penicillin ◽  
Angle Spinning ◽  
Low Symmetry

Structural Properties of a Dimeric Phenylcyanamidocopper(I) Complex, [{Cu(PPh3)2(C6H5NCN)}2]

2000 ◽  
Vol 53 (12) ◽  
pp. 971 ◽  
Author(s):  
Eric W. Ainscough ◽  
Andrew M. Brodie ◽  
Peter C. Healy ◽  
Joyce M. Waters
Keyword(s):  
Crystal Structure ◽  
Solid State ◽  
Structural Properties ◽  
Structure Determination ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Cross Polarization ◽  
X Ray ◽  
Angle Spinning

The X-ray crystal structure determination of bis[-(phenylcyanamido)bis(triphenylphosphine)copper(I)], [{Cu(PPh3)2(C6H5NCN)}2], (1) is reported. The complex has a centrosymmetric dimeric structure with the phenylcyanamide ligands bridging the copper atoms in a -1,3-fashion. The structure is compared with that of the 4-methylphenylcyanamido complex, [{Cu(PPh3)2(4-MeC6H4NCN)}2] (2), and the differences observed in the Cu–P bond lengths compared with changes in the solid state 31P cross-polarization magic-angle spinning (CPMAS) spectra of the two complexes.

Lewis-Base Adducts of Group I Metal(I) Compounds. XXVI. Solid-State Cross-Polarization Magic-Angle-Spinning 31P N.M.R. and Structural Studies on 1:1 Adducts of Triphenylphosphine With Gold(I) Salts

1987 ◽  
Vol 40 (9) ◽  
pp. 1545 ◽  
Author(s):  
PF Barron ◽  
LM Engelhardt ◽  
PC Healy ◽  
J Oddy ◽  
AH White
Keyword(s):  
Solid State ◽  
Magic Angle Spinning ◽  
Lewis Base ◽  
Magic Angle ◽  
Molecular Formula ◽  
Cross Polarization ◽  
X Ray Diffraction ◽  
X Ray ◽  
Group I ◽  
Angle Spinning

Linear, two-coordinate compounds of molecular formula (PPh3) AuX have been characterized by solid-state and solution 31P n.m.r. spectroscopy, and single-crystal X-ray diffraction techniques. The solid state n.m.r. spectra reveal single, broad resonance lines for X = NO3 (chemical shift 19 ppm , ref. 85% H3PO4), CH3C02 (24 ppm), SCN (36ppm), CN (37 ppm ) and CH3 (47 ppm ) and doublets for X = Cl (27, 33 ppm ), Br (28, 36 ppm ) and I (34, 38 ppm ), the latter three spectra being recorded at 121.47 MHz and 161.96 MHz. Solution spectra show relatively sharp single resonances for each compound with 6 values generally slightly higher than in the solid state. Crystal data are reported for X = NO3, space gro )p P21/c, a 8 895(9), b 10.117(8), c 19.57(2) �; β 97.43(8)�, Au-P,O = 2.199(5), 2.02(1) �. Crystals of compounds with X = Br, I and SCN are isomorphous with the AuCl compound, belonging to space group 212121. For X = Br, a 12.479(5), b 13.45(1), c 10.0!2(8) �; Au-P, Br = 2.252(6), 2.407(2) �. For X = I, a 12.529(8), b 13.870(5), c 10.188(4) �; Au-P, I = 2.254(5), 2.556(2) �. For X = SCN, a 12.257(5), b 13.776(8), c 10.754(6) �; Au-P, S = 2.252(7), 2.304(7) �.

scholarly journals Structural changes of TasA in biofilm formation ofBacillus subtilis

2018 ◽  
Vol 115 (13) ◽  
pp. 3237-3242 ◽  
Author(s):  
Anne Diehl ◽  
Yvette Roske ◽  
Linda Ball ◽  
Anup Chowdhury ◽  
Matthias Hiller ◽  
...  
Keyword(s):  
Structural Change ◽  
Structural Changes ◽  
Analytical Ultracentrifugation ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
X Ray ◽  
X Ray Crystallography ◽  
Angle Spinning

Microorganisms form surface-attached communities, termed biofilms, which can serve as protection against host immune reactions or antibiotics.Bacillus subtilisbiofilms contain TasA as major proteinaceous component in addition to exopolysaccharides. In stark contrast to the initially unfolded biofilm proteins of other bacteria, TasA is a soluble, stably folded monomer, whose structure we have determined by X-ray crystallography. Subsequently, we characterized in vitro different oligomeric forms of TasA by NMR, EM, X-ray diffraction, and analytical ultracentrifugation (AUC) experiments. However, by magic-angle spinning (MAS) NMR on live biofilms, a swift structural change toward only one of these forms, consisting of homogeneous and protease-resistant, β-sheet–rich fibrils, was observed in vivo. Thereby, we characterize a structural change from a globular state to a fibrillar form in a functional prokaryotic system on the molecular level.

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