Comparison of two different lysozyme types under native and crystallization conditions using two-dimensional NMR and dynamic light scattering.
In order to elucidate differences observed in the aggregation kinetics of hen-egg white lysozyme under crystallization conditions we have undertaken a comparative study of the enzyme marketed by Seikagaku and Sigma companies. When the crystallization of the two lysozyme preparations is followed by time-resolved dynamic light scattering, the structural differences are also observed under native conditions in the early nucleation kinetics. The differences are manifested in the formation rates of macroscopic crystals, but do not influence the morphology of the typical tetragonal lysozyme crystal. Using two-dimensional NMR we have followed the differences in the native-like solution structure of the two preparations, while the primary sequence and molecular mass are identical. According to the published structure of tetragonal lysozyme crystal the largest deviations were found for the residues involved in the intermolecular interactions in crystal structure.
Poznański
Jaroslaw
J
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5A, 02-106 Warsaw, Poland. jarek@ibb.waw.pl
Georgalis
Yannis
Y
Wehr
Lorin
L
Saenger
Wolfram
W
Zielenkiewicz
Piotr
P
D000818:Animals; D002645:Chickens; D003460:Crystallization; D005260:Female; D007700:Kinetics; D008027:Light; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D012542:Scattering, Radiation; D021241:Spectrometry, Mass, Electrospray Ionization
C421864:hen egg lysozyme; D009113:Muramidase