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X‐Ray Study of Herbaspirilum Seropedicae GlnB Protein Adsorbed on Silicon
Author(s) -
Lubambo Adriana Freire,
Benelli Elaine Machado,
Mazzaro Irineu,
Yokaichyia Fabiano,
Giles Carlos,
de Camargo Paulo César
Publication year - 2006
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/masy.200651319
Subject(s) - silicon , diffraction , crystallography , atomic force microscopy , materials science , globular protein , chemistry , nanotechnology , optics , optoelectronics , physics
GlnB‐Hs protein is a globular member of PII‐like family involved in the nitrogen control fixation in diazothoph organisms like H. seropedicae . In this work, GlnB‐Hs is deposited by spin‐coating on Si (111) and its self‐assembling is investigated by AFM (atomic force microscopy) and X‐ray at grazing incidence angles. GlnB‐Hs forms circular 100 nm to 150 nm wide face‐up donut shaped protein aggregates on silicon. Reflectivity and diffraction profiles from the protein deposits on Si(111) and Si(100), suggest ordered domains that are stable under the X‐ray beam and have d‐spacing compatible with protein dimensions already determined by classical protein crystallography.