Open AccessProtein crystallization by using porous glass substrate
Author(s) -
Rong L.,
Komatsu H.,
Yoshizaki I.,
Kadowaki A.,
Yoda S.
Publication year - 2003
Publication title -
journal of synchrotron radiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 99
ISSN - 1600-5775
DOI - 10.1107/s0909049503023525
Subject(s) - nucleation , thaumatin , crystallization , materials science , porosity , chemical engineering , porous glass , substrate (aquarium) , protein crystallization , lysozyme , crystallography , chemistry , composite material , organic chemistry , biochemistry , oceanography , engineering , gene , geology
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.