@misc{oai:repo.qst.go.jp:00080218,
 author = {Kosaka, Megumi and Yamada, Hidenori and Futami, Junichiro and Tada, Hiroko and Imamura, Koreyoshi and Tamada, Taro and Tamada, Taro},
 month = {Jul},
 note = {A high quality single crystallization of protein is indispensable for X-ray crystallography. However, it is difficult to obtain the crystal, and the crystallization process for the X-ray crystallography needs to be improved. Based on the assumption that hard-to-crystallize protein may be less likely to form the intermolecular interactions responsible for the ordered molecular arrays, the crystal lattice engineering has been applied to design the protein molecular surface so as to form the intermolecular hydrophobic packing. First, the substitution with leucine was found to alter the crystal system of RNase A. Next hard-to-crystalize hRNase 1 was investigated focusing the impacts of the other (hydrophobic) amino acid residues on the crystallization behavior. Seven types of hRNase 1, mutated on 24T, 28Q, 31R, and 32R or 52V, 53D, 56N, 59F were prepared and examined for their crystallization behavior. Three recombinant hRNase 1, replaced to phenylalanine (3F-hRNase 1), valine (3V-), and alanine (3A-), exhibited the crystallization. This indicates the facilitation of hRNase 1 crystallization by the insertion of hydrophobic amino acid residues for the intermolecular packing sites. The obtained recombinant hRNase 1 crystals were collected for their X-ray diffraction data at the large synchrotron radiation facility SPring-8, BL26B1 and BL38B1., The 20th Annual Meeting of the Protein Science Society of Japan},
 title = {Impacts Of The Introduction Of Hydrophobic Residues On The Protein Crystallization},
 year = {2020}
}