Characterisation of an improved two-dimensional p22121 crystal from bovine rhodopsin.
作者： Angelika Krebs , Claudio Villa , Patricia C Edwards , Gebhard F.X Schertler
关键词:
摘要: Dialysis of rhodopsin isolated from bovine rod outer segments resulted in the formation a new two-dimensional crystal form suitable for electron crystallography. The crystals obtained were tubular or single layers and showedp 22121symmetry (a=60.6(±0.8) A,b=86.3(±1.6) A). For first time size order allowed us to take diffraction patterns showing spots resolution about 3.5 A. Images recorded at liquid nitrogen temperature using high voltage field emission microscope. Out large number images 20 crystalline areas selected processed with MRC image processing software. A projection structure 5 was calculated amplitudes phases extracted these images. achieved exceeds all previously structures frog, squid crystals. In this map small differences are observed compared previous maps. Helix seems be even more highly tilted between arc-shaped feature helix peak is present suggesting that 3 prolonging towards 5. These observations agreement latest model three-dimensional arrangement rhodopsin. as well availability data suggest there good possibility collect calculate an improved
elsevier.com
sci-hub.se 参考文章(37)
Willem J. De Grip, Purification of bovine rhodopsin over concanavalin A--sepharose. Methods in Enzymology. ,vol. 81, pp. 197- 207 ,(1982) , 10.1016/S0076-6879(82)81032-X
J.M. Baldwin, The probable arrangement of the helices in G protein‐coupled receptors. The EMBO Journal. ,vol. 12, pp. 1693- 1703 ,(1993) , 10.1002/J.1460-2075.1993.TB05814.X
Paul A. Hargrave, J. Hugh McDowell, Rhodopsin and Phototransduction International Review of Cytology-a Survey of Cell Biology. ,vol. 137, pp. 49- 97 ,(1993) , 10.1016/S0074-7696(08)62600-5
Vinzenz M. Unger, Paul A. Hargrave, Joyce M. Baldwin, Gebhard F. X. Schertler, Arrangement of rhodopsin transmembrane α-helices Nature. ,vol. 389, pp. 203- 206 ,(1997) , 10.1038/38316
H Shichi, M S Lewis, F Irreverre, A L Stone, Biochemistry of Visual Pigments I. PURIFICATION AND PROPERTIES OF BOVINE RHODOPSIN Journal of Biological Chemistry. ,vol. 244, pp. 529- 536 ,(1969) , 10.1016/S0021-9258(18)94389-9
S S Karnik, H G Khorana, Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. Journal of Biological Chemistry. ,vol. 265, pp. 17520- 17524 ,(1990) , 10.1016/S0021-9258(18)38195-X
Catherine D. Strader, Tung Ming Fong, Michael P. Grazlano, Michael R. Tota, The family of G-protein-coupled receptors. The FASEB Journal. ,vol. 9, pp. 745- 754 ,(1995) , 10.1096/FASEBJ.9.9.7601339
R.A. Crowther, R. Henderson, J.M. Smith, MRC Image Processing Programs Journal of Structural Biology. ,vol. 116, pp. 9- 16 ,(1996) , 10.1006/JSBI.1996.0003
P.A. Bullough, P.A. Tulloch, High-resolution spot-scan electron microscopy of microcrystals of an α-helical coiled-coil protein Journal of Molecular Biology. ,vol. 215, pp. 161- 173 ,(1990) , 10.1016/S0022-2836(05)80101-9
V.M. Unger, G.F. Schertler, Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy Biophysical Journal. ,vol. 68, pp. 1776- 1786 ,(1995) , 10.1016/S0006-3495(95)80354-1