A practical guide to the use of monolayer purification and affinity grids

Methods in Enzymology

Volumn 481, Issue C, 2010, Pages 83-107

  Kelly, Deborah F ^a   Dukovski, Danijela ^a,b   Walz, Thomas ^a,b  

^a HARVARD MEDICAL SCHOOL   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN 9; CELL EXTRACT; MEMBRANE PROTEIN; NOTCH RECEPTOR; RIBOSOME PROTEIN; RNA POLYMERASE;

BOOK; CRYSTALLOGRAPHY; ELECTRON MICROSCOPY; LIPID MONOLAYER; MASS SPECTROMETRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MICROARRAY; PROTEIN PURIFICATION;

EID: 77957228396     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)81004-3     Document Type: Chapter

References (44)

1. Abraham J., Corbett K.D., Farzan M., Choe H., Harrison S.C. Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses. Nat. Struct. Mol. Biol. 2010, 4:438-444.
2. Al-Kurdi R., Gulino-Debrac D., Martel L., Legrand J.F., Renault A., Hewat E., Venien-Bryan C. A soluble VE-cadherin fragment forms 2D arrays of dimers upon binding to a lipid monolayer. J. Mol. Biol. 2004, 337:881-892.
3. Asturias F.J., Kornberg R.D. A novel method for transfer of two-dimensional crystals from the air/water interface to specimen grids. EM sample preparation/lipid-layer crystallization. J. Struct. Biol. 1995, 114:60-66.
4. Asturias F.J., Chang W., Li Y., Kornberg R.D. Electron crystallography of yeast RNA polymerase II preserved in vitreous ice. Ultramicroscopy 1998, 70:133-143.
5. Avila-Sakar A.J., Chiu W. Visualization of β-sheets and side-chain clusters in two-dimensional periodic arrays of streptavidin on phospholipid monolayers by electron crystallography. Biophys. J. 1996, 70:57-68.
6. Azubel M., Wolf S.G., Sperling J., Sperling R. Three-dimensional structure of the native spliceosome by cryo-electron microscopy. Mol. Cell 2004, 15:833-839.
7. Brisson A., Mosser G., Huber R. Structure of soluble and membrane-bound human annexin V. J. Mol. Biol. 1991, 220:199-203.
8. Carragher B., Voss N.R., Potter C.S., Smith R. Software tools for molecular microscopy: An open-text Wikibook. Methods Enzymol. 2010, 482:381-392.
9. Darst S.A., Kubalek E.W., Kornberg R.D. Three-dimensional structure of Escherichia coli RNA polymerase holoenzyme determined by electron crystallography. Nature 1989, 340:730-732.
10. De Carlo S., Stark H. Cryo-negative staining of macromolecular assemblies. Methods Enzymol. 2010, 481:127-145.
11. Ganser B.K., Cheng A., Sundquist W.I., Yeager M. Three-dimensional structure of the M-MuLV CA protein on a lipid monolayer: A general model for retroviral capsid assembly. EMBO J. 2003, 22:2886-2892.
12. Golas M.M., Sander B., Will C.L., Luhrmann R., Stark H. Molecular architecture of the multiprotein splicing factor SF3b. Science 2003, 300:980-984.
13. Hussein W.M., Ross B.P., Landsberg M.J., Levy D., Hankamer B., McGeary R.P. Synthesis of nickel-chelating fluorinated lipids for protein monolayer crystallizations. J. Org. Chem. 2009, 74:1473-1479.
14. Jurica M.S., Sousa D., Moore M.J., Grigorieff N. Three-dimensional structure of C complex spliceosomes by electron microscopy. Nat. Struct. Mol. Biol. 2004, 11:265-269.
15. Kastner B., Fischer N., Golas M.M., Sander B., Dube P., Boehringer D., Hartmuth K., Deckert J., Hauer F., Wolf E., Uchtenhagen H., Urlaub H., et al. GraFix: Sample preparation for single-particle electron cryomicroscopy. Nat. Methods 2008, 5:53-55.
16. Kelly D.F., Taylor D.W., Bakolitsa C., Bobkov A.A., Bankston L., Liddington R.C., Taylor K.A. Structure of the α-actinin-vinculin head domain complex determined by cryo-electron microscopy. J. Mol. Biol. 2006, 357:562-573.
17. Kelly D.F., Dukovski D., Walz T. Monolayer purification: A rapid method for isolating protein complexes for single-particle electron microscopy. Proc. Natl. Acad. Sci. USA 2008, 105:4703-4708.
18. Kelly D.F., Abeyrathne P.D., Dukovski D., Walz T. The Affinity Grid: A pre-fabricated EM grid for monolayer purification. J. Mol. Biol. 2008, 382:423-433.
19. Kelly D.F., Lake R.J., Middlekoop T.J., Fan H.-Y., Artavanis-Tsakonas S., Walz T. Molecular structure and dimeric organization of the Notch extracellular domain as revealed by electron microscopy. PLoS ONE 2010, 5, e10532.
20. Kelly D.F., Dukovski D., Walz T. Strategy for the use of affinity grids to prepare non-His-tagged macromolecular complexes for single-particle electron microscopy. J. Mol. Biol. 2010, 400:675-681.
21. Kettenberger H., Armache K.J., Cramer P. Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Mol. Cell 2004, 16:955-965.
22. Klaholz B.P., Pape T., Zavialov A.V., Myasnikov A.G., Orlova E.V., Vestergaard B., Ehrenberg M., van Heel M. Structure of the Escherichia coli ribosomal termination complex with release factor 2. Nature 2003, 421:90-94.
23. Kubalek E.W., Le Grice S.F., Brown P.O. Two-dimensional crystallization of histidine-tagged, HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid. J. Struct. Biol. 1994, 113:117-123.
24. Lebeau L., Lach F., Venien-Bryan C., Renault A., Dietrich J., Jahn T., Palmgren M.G., Kuhlbrandt W., Mioskowski C. Two-dimensional crystallization of a membrane protein on a detergent-resistant lipid monolayer. J. Mol. Biol. 2001, 308:639-647.
25. Levy D., Chami M., Rigaud J.L. Two-dimensional crystallization of membrane proteins: The lipid layer strategy. FEBS Lett. 2001, 504:187-193.
26. McDowall A.W., Dobro M.J., Melanson L.A., Jensen G.J. Plunge freezing for electron cryomicroscopy. Methods Enzymol. 2010, 481:63-82.
27. Medalia O., Typke D., Hegerl R., Angenitzki M., Sperling J., Sperling R. Cryoelectron microscopy and cryoelectron tomography of the nuclear pre-mRNA processing machine. J. Struct. Biol. 2002, 138:74-84.
28. Muller S.A., Engel A. Structure and mass analysis by scanning transmission electron microscopy. Micron 2001, 32:21-31.
29. Norville J.E., Kelly D.F., Knight T.F., Belcher A.M., Walz T. 7Ȧ projection map of the S-layer protein sbpA obtained with trehalose-embedded monolayer crystals. J. Struct. Biol. 2007, 160:313-323.
30. Ohi M., Li Y., Cheng Y., Walz T. Negative staining and image classification-Powerful tools in modern electron microscopy. Biol. Proced. Online 2004, 6:23-34.
31. Olofsson A., Kaveus U., Hacksell I., Thelestam M., Hebert H. Crystalline layers and three-dimensional structure of Staphylococcus aureus α-toxin. J. Mol. Biol. 1990, 214:299-306.
32. Qin H., Liu Z., Sui S.F. Two-dimensional crystallization of avidin on biotinylated lipid monolayers. Biophys. J. 1995, 68:2493-2496.
33. Radermacher M., Wagenknecht T., Verschoor A., Frank J. Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J. Microsc. 1987, 146:113-136.
34. Sjoquist J., Stalenheim G. Protein A from Staphylococcus aureus. IX. Complement-fixing activity of protein A-IgG complexes. J. Immunol. 1969, 103:467-473.
35. Stagg S.M., Lander G.C., Pulokas J., Fellmann D., Cheng A., Quispe J.D., Mallick S.P., Avila R.M., Carragher B., Potter C.S. Automated cryoEM data acquisition and analysis of 284742 particles of GroEL. J. Struct. Biol. 2006, 155:470-481.
36. Stroupe M.E., Xu C., Goode B.L., Grigorieff N. Actin filament labels for localizing protein components in large complexes viewed by electron microscopy. RNA 2009, 15:244-248.
37. 2+ -dependent actin binding. J. Mol. Biol. 2001, 310:845-858.
38. Taylor K.A., Glaeser R.M. Retrospective on the early development of cryoelectron microscopy of macromolecules and a prospective on opportunities for the future. J. Struct. Biol. 2008, 163:214-223.
39. Taylor K.A., Taylor D.W. Projection image of smooth muscle α-actinin from two-dimensional crystals formed on positively charged lipid layers. J. Mol. Biol. 1993, 230:196-205.
40. Thess A., Hutschenreiter S., Hofmann M., Tampe R., Baumeister W., Guckenberger R. Specific orientation and two-dimensional crystallization of the proteasome at metal-chelating lipid interfaces. J. Biol. Chem. 2002, 277:36321-36328.
41. Thomas D., Schultz P., Steven A.C., Wall J.S. Mass analysis of biological macromolecular complexes by STEM. Biol. Cell 1994, 80:181-192.
42. Uzgiris E.E., Kornberg R.D. Two-dimensional crystallization technique for imaging macromolecules, with application to antigen-antibody-complement complexes. Nature 1983, 301:125-129.
43. Venien-Bryan C., Balavoine F., Toussaint B., Mioskowski C., Hewat E.A., Helme B., Vignais P.M. Structural study of the response regulator HupR from Rhodobacter capsulatus. Electron microscopy of two-dimensional crystals on a nickel-chelating lipid. J. Mol. Biol. 1997, 274:687-692.
44. 2+ ions on its interaction with lipid layers. J. Struct. Biol. 1992, 109:129-141.