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Impacts Of The Introduction Of Hydrophobic Residues On The Protein Crystallization
https://repo.qst.go.jp/records/80218
https://repo.qst.go.jp/records/802187417867a-e8c3-4ae0-904a-1f90efdb25ac
| Item type | 会議発表用資料 / Presentation(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2020-07-16 | |||||
| タイトル | ||||||
| タイトル | Impacts Of The Introduction Of Hydrophobic Residues On The Protein Crystallization | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_c94f | |||||
| 資源タイプ | conference object | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
Kosaka, Megumi
× Kosaka, Megumi× Yamada, Hidenori× Futami, Junichiro× Tada, Hiroko× Imamura, Koreyoshi× Tamada, Taro× Tamada, Taro |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | 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. | |||||
| 会議概要（会議名, 開催地, 会期, 主催者等） | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | The 20th Annual Meeting of the Protein Science Society of Japan | |||||
| 発表年月日 | ||||||
| 日付 | 2020-07-15 | |||||
| 日付タイプ | Issued | |||||
