ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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言語種別 | 英語 |
発行・発表の年月 | 2004/04 |
形態種別 | 研究論文 |
査読 | 査読あり |
標題 | Crystallization and preliminary X-ray diffraction analysis of the hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum |
執筆形態 | その他 |
掲載誌名 | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY |
出版社・発行元 | BLACKWELL MUNKSGAARD |
巻・号・頁 | 60(60(4)),pp.715-717 |
担当区分 | 最終著者,責任著者 |
著者・共著者 | MW Bhuiya,H Sakuraba,K Yoneda,T Ohshima,T Imagawa,N Katunuma,H Tsuge |
概要 | NAD-dependent glutamate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum was crystallized in the apo- and holoenzyme forms. Crystals were obtained using 2-propanol and polyethylene glycol MME 550 as precipitants for the apoenzyme and holoenzyme, respectively. The apoenzyme crystals belong to the trigonal space group P3(1)21 or its enantiomorph P3(2)21. The asymmetric unit contains three subunits; the values of the Matthews coef'cient (V-M) and the solvent content are 2.9 Angstrom(3) Da(-1) and 57%, respectively. A native data set was collected to a highest resolution limit of 4.0 Angstrom on an in-house X-ray source using a rotating-anode generator (overall R-sym of 12.3% and completeness of 97%). The holoenzyme crystals belong to the orthorhombic space group P2(1)2(1)2(1); the asymmetric unit contains one hexamer, giving a VM of 2.79 Angstrom(3) Da(-1) and a solvent content of 55%. Native and derivative data sets were collected. The crystals diffract to a maximum resolution of 2.8 Angstrom on the KEK-NW12 beamline at the Photon Factory and gave a data set with an overall R-sym of 7.9% and a completeness of 91%. Attempts are being made to solve the structure by the SIRAS method. |
DOI | 10.1107/S0907444904001854 |
ISSN | 0907-4449 |