Preparation of a Cross-Linked Porous Protein Crystal Containing Ru Carbonyl Complexes as a CO-Releasing Extracellular Scaffold

2014 ◽  
Vol 54 (1) ◽  
pp. 215-220 ◽  
Author(s):  
Hiroyasu Tabe ◽  
Kenta Fujita ◽  
Satoshi Abe ◽  
Masahiko Tsujimoto ◽  
Takahiro Kuchimaru ◽  
...  
Keyword(s):  
Protein Crystal ◽  
Carbonyl Complexes ◽  
Extracellular Scaffold

Spot-scan imaging of ice-embedded catalase crystal on a slow-scan CCD camera in a 400-kV electron cryomicroscope

1994 ◽  
Vol 52 ◽  
pp. 98-99
Author(s):  
Wah Chiu ◽  
Michael Sherman ◽  
Jaap Brink
Keyword(s):  
Electron Diffraction ◽  
Ccd Camera ◽  
Protein Crystal ◽  
Modulation Transfer ◽  
Measured Intensity ◽  
3 Dimensional ◽  
Dimensional Reconstruction ◽  
Diffraction Patterns ◽  
Complex Crystal

In protein electron crystallography, both low dose electron diffraction patterns and images are needed to provide accurate amplitudes and phases respectively for a 3-dimensional reconstruction. We have demonstrated that the Gatan 1024x1024 model 679 slow-scan CCD camera is useful to record electron diffraction intensities of glucose-embedded crotoxin complex crystal to 3 Å resolution. The quality of the electron diffraction intensities is high on the basis of the measured intensity equivalence ofthe Friedel-related reflections. Moreover, the number of patterns recorded from a single crystal can be as high as 120 under the constraints of radiation damage and electron statistics for the reflections in each pattern.A limitation of the slow-scan CCD camera for recording electron images of protein crystal arises from the relatively large pixel size, i.e. 24 μm (provided by Gatan). The modulation transfer function of our camera with a P43 scintillator has been determined for 400 keV electrons and shows an amplitude fall-off to 0.25 at 1/60 μm−1.

MULTIPLE SCATTERING EFFECTS IN THE COBALT K-EDGE EXAFS OF METAL CARBONYL COMPLEXES

1986 ◽  
Vol 47 (C8) ◽  
pp. C8-589-C8-592
Author(s):  
N. BINSTED ◽  
S. L. COOK ◽  
J. EVANS ◽  
R. J. PRICE ◽  
G. N. GREAVES
Keyword(s):  
Multiple Scattering ◽  
Metal Carbonyl ◽  
Carbonyl Complexes ◽  
Metal Carbonyl Complexes ◽  
Scattering Effects ◽  
Multiple Scattering Effects

Microgravity protein crystal growth

1991 ◽  
Author(s):  
CHARLES BUGG ◽  
LAWRENCE DELUCAS
Keyword(s):  
Crystal Growth ◽  
Protein Crystal ◽  
Protein Crystal Growth

Redox Potential - (Electronic) Structure Relationships in 18- and 17-Electron Mononitrile (or Monocarbonyl) Diphosphine Complexes of Re and Fe

2001 ◽  
Vol 66 (1) ◽  
pp. 139-154 ◽  
Author(s):  
M. Fátima C. Guedes Da Silva ◽  
Luísa M. D. R. S. Martins ◽  
João J. R. Fraústo Da Silva ◽  
Armando J. L. Pombeiro
Keyword(s):  
Cyclic Voltammetry ◽  
Electronic Structure ◽  
Binding Sites ◽  
Closed Shell ◽  
Carbonyl Complexes ◽  
Metal Centre ◽  
Pt Electrode ◽  
Metal Site ◽  
Oxidation Potentials ◽  
First Time

The organonitrile or carbonyl complexes cis-[ReCl(RCN)(dppe)2] (1) (R = 4-Et2NC6H4 (1a), 4-MeOC6H4 (1b), 4-MeC6H4 (1c), C6H5 (1d), 4-FC6H4 (1e), 4-ClC6H4 (1f), 4-O2NC6H4 (1g), 4-ClC6H4CH2 (1h), t-Bu (1i); dppe = Ph2PCH2CH2PPh2), or cis-[ReCl(CO)(dppe)2] (2), as well as trans-[FeBr(RCN)(depe)2]BF4 (3) (R = 4-MeOC6H4 (3a), 4-MeC6H4 (3b), C6H5 (3c), 4-FC6H4 (3d), 4-O2NC6H4 (3e), Me (3f), Et (3g), 4-MeOC6H4CH2 (3h); depe = Et2PCH2CH2PEt2), novel trans-[FeBr(CO)(depe)2]BF4 (4) and trans-[FeBr2(depe)2] (5) undergo, as revealed by cyclic voltammetry at a Pt-electrode and in aprotic non-aqueous medium, two consecutive reversible or partly reversible one-electron oxidations assigned as ReI → ReII → ReIII or FeII → FeIII → FeIV. The corresponding values of the oxidation potentials IE1/2ox and IIE1/2ox (waves I and II, respectively) correlate with the Pickett's and Lever's electrochemical ligand and metal site parameters. This allows to estimate these parameters for the various nitrile ligands, depe and binding sites (for the first time for a FeIII/IV couple). The electrochemical ligand parameter show dependence on the "electron-richness" of the metal centre. The values of IE1/2ox for the ReI complexes provide some supporting for a curved overall relationship with the sum of Lever's electrochemical ligand parameter. The Pickett parametrization for closed-shell complexes is extended now also to 17-electron complexes, i.e. with the 15-electron ReII and FeIII centres in cis-{[ReCl(dppe)2]}+ and trans-{FeBr(depe)2}2+, respectively.

Transition Metal Carbonyl Complexes of an N-Heterocyclic Carbene Stabilized Silyliumylidene Ion

2019 ◽  
Vol 58 (21) ◽  
pp. 14931-14937 ◽  
Author(s):  
Philipp Frisch ◽  
Tibor Szilvási ◽  
Amelie Porzelt ◽  
Shigeyoshi Inoue
Keyword(s):  
Transition Metal ◽  
Metal Carbonyl ◽  
Carbonyl Complexes ◽  
Metal Carbonyl Complexes

Resolution of a protein sequence ambiguity by X-ray crystallographic and mass spectrometric methods

1992 ◽  
Vol 25 (2) ◽  
pp. 205-210 ◽  
Author(s):  
L. J. Keefe ◽  
E. E. Lattman ◽  
C. Wolkow ◽  
A. Woods ◽  
M. Chevrier ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Electron Density ◽  
Mass Spectrometric ◽  
Amino Acid Sequences ◽  
Data Matrix ◽  
Protein Crystal ◽  
Insertion Mutant ◽  
Laser Desorption Mass Spectrometry ◽  
X Ray

Ambiguities in amino acid sequences are a potential problem in X-ray crystallographic studies of proteins. Amino acid side chains often cannot be reliably identified from the electron density. Many protein crystal structures that are now being solved are simple variants of a known wild-type structure. Thus, cloning artifacts or other untoward events can readily lead to cases in which the proposed sequence is not correct. An example is presented showing that mass spectrometry provides an excellent tool for analyzing suspected errors. The X-ray crystal structure of an insertion mutant of Staphylococcal nuclease has been solved to 1.67 Å resolution and refined to a crystallographic R value of 0.170 [Keefe & Lattman (1992). In preparation]. A single residue has been inserted in the C-terminal α helix. The inserted amino acid was believed to be an alanine residue, but the final electron density maps strongly indicated that a glycine had been inserted instead. To confirm the observations from the X-ray data, matrix-assisted laser desorption mass spectrometry was employed to verify the glycine insertion. This mass spectrometric technique has sufficient mass accuracy to detect the methyl group that distinguishes glycine from alanine and can be extended to the more common situation in which crystallographic measurements suggest a problem with the sequence, but cannot pinpoint its location or nature.

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