scholarly journals Time-dependent X-ray diffraction studies on urea/hen egg white lysozyme complexes reveal structural changes that indicate onset of denaturation

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Tushar Raskar ◽  
Sagar Khavnekar ◽  
Madhusoodan Hosur
Keyword(s):  
Structural Changes ◽  
Egg White ◽  
Time Dependent ◽  
Hen Egg White Lysozyme ◽  
X Ray Diffraction ◽  
X Ray ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

ESI mass spectrometry and X-ray diffraction studies of adducts between anticancer platinum drugs and hen egg white lysozyme

2007 ◽  
pp. 156-158 ◽  
Author(s):  
Angela Casini ◽  
Guido Mastrobuoni ◽  
Claudia Temperini ◽  
Chiara Gabbiani ◽  
Simona Francese ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Egg White ◽  
Platinum Drugs ◽  
Hen Egg White Lysozyme ◽  
X Ray Diffraction ◽  
X Ray ◽  
Egg White Lysozyme ◽  
Esi Mass Spectrometry ◽  
Hen Egg White ◽  
Hen Egg

Analysis of polycrystallinity in hen egg-white lysozyme using a pnCCD

2012 ◽  
Vol 45 (3) ◽  
pp. 517-522 ◽  
Author(s):  
Sebastian Send ◽  
Ali Abboud ◽  
Wolfram Leitenberger ◽  
Manfred S. Weiss ◽  
Robert Hartmann ◽  
...  
Keyword(s):  
Sample Surface ◽  
Egg White ◽  
Hen Egg White Lysozyme ◽  
X Ray ◽  
Lattice Constants ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Diffraction Patterns ◽  
Crystalline Domains ◽  
Hen Egg

A crystal of hen egg-white lysozyme was analyzed by means of energy-dispersive X-ray Laue diffraction with white synchrotron radiation at 2.7 Å resolution using a pnCCD detector. From Laue spots measured in a single exposure of the arbitrarily oriented crystal, the lattice constants of the tetragonal unit cell could be extracted with an accuracy of about 2.5%. Scanning across the sample surface, Laue images with split reflections were recorded at various positions. The corresponding diffraction patterns were generated by two crystalline domains with a tilt of about 1° relative to each other. The obtained results demonstrate the potential of the pnCCD for fast X-ray screening of crystals of macromolecules or proteins prior to conventional X-ray structure analysis. The described experiment can be automatized to quantitatively characterize imperfect single crystals or polycrystals.

Crystal distortion of monoclinic hen egg-white lysozyme crystals using X-ray digital topography

2014 ◽  
Vol 401 ◽  
pp. 238-241
Author(s):  
Kei Wako ◽  
Daiki Fujii ◽  
Shiro Tsukashima ◽  
Takeharu Kishi ◽  
Masaru Tachibana ◽  
...  
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
X Ray ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Lysozyme Crystals ◽  
Hen Egg

The metalation of hen egg white lysozyme impacts protein stability as shown by ion mobility mass spectrometry, differential scanning calorimetry, and X-ray crystallography

2017 ◽  
Vol 53 (30) ◽  
pp. 4246-4249 ◽  
Author(s):  
Matthew P. Sullivan ◽  
Michael Groessl ◽  
Samuel M. Meier ◽  
Richard L. Kingston ◽  
David C. Goldstone ◽  
...  
Keyword(s):  
Ion Mobility ◽  
Egg White ◽  
Ion Mobility Mass Spectrometry ◽  
Hen Egg White Lysozyme ◽  
Scanning Calorimetry ◽  
X Ray ◽  
X Ray Crystallography ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

Metalation of lysozyme with anticancer organometallics results in protein destabilisation, probably relevant in metallodrug mode of action.

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