与RNA及一种ATP类似物复合的Vasa解旋酶结构域的结晶及初步X射线分析。
Crystallization and preliminary X-ray analysis of the helicase domains of Vasa complexed with RNA and an ATP analogue.
作者信息
Sengoku Toru, Nureki Osamu, Dohmae Naoshi, Nakamura Akira, Yokoyama Shigeyuki
机构信息
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
出版信息
Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):320-2. doi: 10.1107/S0907444903025897. Epub 2004 Jan 23.
The helicase fragment of Vasa was purified and its RNA-binding activity was examined by a UV cross-linking assay. The fragment was crystallized in complex with poly(U) RNA (U(10)) and a non-hydrolyzable analogue of ATP. The crystal belonged to space group P2(1), with unit-cell parameters a = 71.06, b = 142.35, c = 130.47 A, beta = 90.86 degrees. The cryocooled crystal diffracted to about 2.2 A using synchrotron radiation from station BL41XU at SPring-8.
纯化了Vasa解旋酶片段，并通过紫外线交联试验检测其RNA结合活性。该片段与聚（U）RNA（U(10)）和ATP的不可水解类似物形成复合物后结晶。晶体属于空间群P2(1)，晶胞参数为a = 71.06，b = 142.35，c = 130.47 Å，β = 90.86°。使用SPring-8的BL41XU站的同步辐射，该冷冻晶体的衍射分辨率约为2.2 Å。
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