Crystallization and preliminary X-ray analysis of the helicase domains of Vasa complexed with RNA and an ATP analogue.
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.
Sengoku
Toru
T
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
Nureki
Osamu
O
Dohmae
Naoshi
N
Nakamura
Akira
A
Yokoyama
Shigeyuki
S
D000255:Adenosine Triphosphate / Q000737:chemistry*; D000818:Animals; D003432:Cross-Linking Reagents / Q000494:pharmacology; D018360:Crystallography, X-Ray; D053487:DEAD-box RNA Helicases; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000378:metabolism; D006801:Humans; D011072:Poly U; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry*; D020365:RNA Helicases / Q000737:chemistry*; D012333:RNA, Messenger / Q000378:metabolism; D014466:Ultraviolet Rays
D003432:Cross-Linking Reagents; D029721:Drosophila Proteins; D012333:RNA, Messenger; D011072:Poly U; D012313:RNA; D000255:Adenosine Triphosphate; C498288:DDX4 protein, human; C088269:vas protein, Drosophila; D053487:DEAD-box RNA Helicases; D020365:RNA Helicases