Abstract
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 (in) 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. Copyright © 2006 WILEY-VCH Verlag GmbH & Co. KGaA.
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Lubambo, A. F., Benelli, E. M., Mazzaro, I., Yokaichyia, F., Giles, C., & De Camargo, P. C. (2006). X-ray study of herbaspirilum seropedicae GlnB protein adsorbed on silicon. In Macromolecular Symposia (Vol. 245–246, pp. 140–146). Wiley-VCH Verlag. https://doi.org/10.1002/masy.200651319
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