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Observation of crystal growth of lysozyme protein crystals by atomic force microscopy
Author(s) -
Gvozdev N.,
Rashkovich L.,
Yaminsky I.
Publication year - 2000
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/1521-3900(200010)160:1<49::aid-masy49>3.0.co;2-7
Subject(s) - nucleation , orthorhombic crystal system , lysozyme , atomic force microscopy , crystallography , protein crystallization , conductive atomic force microscopy , crystal (programming language) , materials science , crystal growth , resolution (logic) , chemical physics , chemistry , nanotechnology , crystal structure , crystallization , computer science , biochemistry , programming language , organic chemistry , artificial intelligence
Surface structure and the propagation of elementary growth layers over the (010) face of orthorhombic lysozyme crystal is examined at a molecular‐scale resolution by the method of atomic force microscopy (AFM). The steps have a small number of kinks spaced by about 150 growth units. The step motion occurs via successive deposition of rows of growth units. The data obtained are discussed in terms of the model of one‐dimensional nucleation.