Protein crystallization by using porous glass substrate.
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.
Rong
L
L
Space Utilization Research Center, National Space Development Agency of Japan, 2-1-1, Sengen Tsukuba, Ibaraki 305-8505, Japan. long.rong@nasda.go.jp
Komatsu
H
H
Yoshizaki
I
I
Kadowaki
A
A
Yoda
S
S
D001052:Apoferritins / Q000138:chemical synthesis / Q000737:chemistry; D003460:Crystallization / Q000379:methods*; D003461:Crystallography / Q000379:methods*; D019281:Dimerization; D005898:Glass / Q000737:chemistry*; D046911:Macromolecular Substances; D008567:Membranes, Artificial; D009113:Muramidase / Q000138:chemical synthesis / Q000737:chemistry; D036103:Nanotechnology / Q000379:methods*; D010940:Plant Proteins / Q000138:chemical synthesis / Q000737:chemistry; D016062:Porosity; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000138:chemical synthesis / Q000737:chemistry*
D046911:Macromolecular Substances; D008567:Membranes, Artificial; D010940:Plant Proteins; D011506:Proteins; C003427:thaumatin protein, plant; D001052:Apoferritins; C421864:hen egg lysozyme; D009113:Muramidase