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Protein crystallization by using porous glass substrate.
- Source :
-
Journal of synchrotron radiation [J Synchrotron Radiat] 2004 Jan 01; Vol. 11 (Pt 1), pp. 27-9. Date of Electronic Publication: 2003 Nov 28. - Publication Year :
- 2004
-
Abstract
- The effects of a commercially available porous glass substrate (Corning Porous Glass No.7930) on the heterogeneous nucleation of proteins [hen egg-white lysozyme (HEWL), thaumatin and apoferritin] have been investigated in order to develop an improved method to facilitate the nucleation of protein crystals. It was found that the porous glass substrate could promote the nucleation at lower supersaturations. The induction time for nucleation decreased, and the crystals obtained from porous glass substrates were larger than those from normal glass substrates. Many pores and channels of 10-100 nm in diameter were observed on the porous glass surface by atomic force microscopy (AFM). It is believed that these pores and channels are crucial for facilitating the nucleation process in this work.
- Subjects :
- Apoferritins chemical synthesis
Apoferritins chemistry
Dimerization
Macromolecular Substances
Muramidase chemical synthesis
Muramidase chemistry
Plant Proteins chemical synthesis
Plant Proteins chemistry
Porosity
Protein Binding
Protein Conformation
Proteins chemical synthesis
Crystallization methods
Crystallography methods
Glass chemistry
Membranes, Artificial
Nanotechnology methods
Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0909-0495
- Volume :
- 11
- Issue :
- Pt 1
- Database :
- MEDLINE
- Journal :
- Journal of synchrotron radiation
- Publication Type :
- Academic Journal
- Accession number :
- 14646126
- Full Text :
- https://doi.org/10.1107/s0909049503023525