High volume confinement in two-photon total-internal-reflection fluorescence correlation spectroscopy
We report results on two-photon total-internal-reflection fluorescence correlation spectroscopy with radially polarized light. The combination of liquid crystal spatial light modulator, providing radi...
We report results on two-photon total-internal-reflection fluorescence correlation spectroscopy with radially polarized light. The combination of liquid crystal spatial light modulator, providing radi...
Four dimensional visualization of highly transient fuel sprays by microsecond quantitative x-ray tomography
An ultrafast x-ray microtomography technique based on synchrotron x rays and a fast-framing x-ray detector was developed to reconstruct the highly transient sprays in four dimensions with microsecond-...
An ultrafast x-ray microtomography technique based on synchrotron x rays and a fast-framing x-ray detector was developed to reconstruct the highly transient sprays in four dimensions with microsecond-...
High resolution pair-distance distribution function P(r) of protein solutions
Appl. Phys. Lett. 94, 083903 (2009); doi:10.1063/1.3089360
Published 26 February 2009
You are not logged in to this journal. Log in
A high resolution pair-distance distribution function P(r) of protein molecules has been obtained from the complete solution scattering curve made by combining accurate small-angle and wide-angle x-ray scattering data out to 2.15 Å resolution. Both indirect and direct Fourier transforms exhibit two distinct peaks at 1.4 and 5.1 Å in P(r). X-ray crystallographic data demonstrate that these peaks correspond to two intramolecular distances: the average bond length between C, N, and O atoms and the pitch of an 
-helix, respectively. Hence some high resolution aspects of the structure and function of a protein may be investigated in a solution.
©2009 American Institute of Physics
-helix, respectively. Hence some high resolution aspects of the structure and function of a protein may be investigated in a solution.
©2009 American Institute of Physics
| History: | Received 11 December 2008; accepted 5 February 2009; published 26 February 2009 |
| Permalink: |
http://link.aip.org/link/?APPLAB/94/083903/1 |
| BUY THIS ARTICLE | (US$24) |
|
|
|
|
Connotea
CiteULike
del.icio.us
BibSonomy
REFERENCES (15)
For access to fully linked references, you need to log in.
For access to fully linked references, you need to Log in.
- J. Trewhella,
Curr. Opin. Struct. Biol. 7, 702 (1997) . - M. H. J. Koch, P. Vachette, and D. I. Svergun,
Q. Rev. Biophys. 36, 147 (2003) . - J. Grossmann,
J. Appl. Crystallogr. 40, s217 (2007) . - T. -y. Teng and K. Moffat,
J. Synchrotron Radiat. 7, 313 (2000) . - D. Borek, S. L. Ginell, M. Cymborowski, W. Minor, and Z. Otwinowski,
J. Synchrotron Radiat. 14, 24 (2007) . - X. Hong and Q. Hao, Rev. Sci. Instrum. 80, 014303 (2009).
- A. P. Hammersley, S. O. Svensson, M. Hanfland, A. N. Fitch, and D. Hausermann,
High Press. Res. 14, 235 (1996) . - R. F. Fischetti, D. J. Rodi, A. Mirza, T. C. Irving, E. Kondrashkina, and L. Makowski,
J. Synchrotron Radiat. 10, 398 (2003) . - W. M. Garrison,
Chem. Rev. (Washington, D.C.) 87, 381 (1987) . - S. Kuwamoto, S. Akiyama, and T. Fujisawa,
J. Synchrotron Radiat. 11, 462 (2004) . - Z. Otwinowski and W. Minor, in Methods in Enzymology, edited by W. C. Carter, Jr. and R. M. Sweet (Academic, New York, 1997), Vol. 276, pp. 307–326.
- D. Svergun,
J. Appl. Crystallogr. 25, 495 (1992) . - Collaborative Computational Project, Number 4,
Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 760 (1994) . - X. Hong, M. Inui, T. Matsusaka, D. Ishikawa, M. Huq Kazi, and K. Tamura,
J. Non-Cryst. Solids 312, 284 (2002) . - R. Kaplow, S. L. Strong, and B. L. Averbach,
Phys. Rev. 138, A1336 (1965) .
