Sengoku Toru, Nureki Osamu, Dohmae Naoshi, Nakamura Akira, Yokoyama Shigeyuki
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
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。
