Characterization of precrystallization aggregation of canavalin by dynamic light scattering.

Published on Jan 1, 1990in Biophysical Journal3.67
· DOI :10.1016/S0006-3495(90)82513-3
Webe Kadima4
Estimated H-index: 4
(UCR: University of California, Riverside),
Alexander McPherson53
Estimated H-index: 53
(UCR: University of California, Riverside)
+ 1 AuthorsFrances Jurnak25
Estimated H-index: 25
(UCR: University of California, Riverside)
The aggregation processes leading to crystallization and precipitation of canavalin have been investigated by dynamic light scattering (DLS) in photon correlation spectroscopy (PCS) mode. The sizes of aggregates formed under various conditions of pH, salt concentration, and protein concentrations were deduced from the correlation functions generated by the fluctuating intensity of light scattered by the solutions of the protein. Results obtained indicate that the barrier to crystallization of canavalin is the formation of the trimer, a species that has been characterized by x-ray crystallographic studies (McPherson, A. 1980. J. Biol. Chem. 255:10472–10480). The dimensions of the trimer in solution are in good agreement with those obtained both from the crystal (McPherson, A. 1980. J. Biol. Chem. 255:10472–10480) and from a low angle x-ray scattering study in solution (Plietz, P., P. Damaschun, J. J. Muller, and B. Schlener. 1983. FEBS [Fed. Eur. Biochem. Soc.] Lett. 162:43–46). Furthermore, under conditions known to lead to the formation of rhombohedral crystals of canavalin, a limiting size is reached at high concentrations of canavalin. The size measured corresponds to an aggregate of trimers making a unit rhombohedral cell consistent with x-ray crystallographic data (McPherson, A. 1980. J. Biol. Chem. 255:10472–10480). Presumably, such aggregates are the nuclei from which crystal growth proceeds. The present study was undertaken primarily to test the potential of DLS (PCS) as a tool for rapid, routine screening to determine the ultimate fate of protein solutions (i.e., crystallization or amorphous precipitation) at an early stage, therefore eliminating the need for long-term visual observation.(ABSTRACT TRUNCATED AT 250 WORDS)
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Cited By68
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Estimated H-index: 9
Over the years, there have been many developments and advances in the field of integral membrane protein research. As important pharmaceutical targets, it is paramount to understand the mechanisms of action that govern their structure–function relationships. However, the study of integral membrane proteins is still incredibly challenging, mostly due to their low expression and instability once extracted from the native biological membrane. Nevertheless, milligrams of pure, stable, and functional...
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Yue Yu2
Estimated H-index: 2
(JLU: Jilin University),
Jianfeng Guo + 3 AuthorsLiying Wang10
Estimated H-index: 10
(JLU: Jilin University)
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Published on Jan 1, 2018in Nanoscale6.97
Mike Sleutel12
Estimated H-index: 12
(Vrije Universiteit Brussel),
Alexander E. S. Van Driessche1
Estimated H-index: 1
Macromolecular phase transitions bear great medical, scientific and industrial relevance, yet the molecular picture of their earliest beginnings is still far from complete. For decades, progress has been hampered by the challenges associated with studying stochastic nucleation phenomena occurring on nanoscopic length scales. In the last 5 years, however, the field has advanced with great strides due to the recent buildout of experimental techniques that allow us to observe details of the nucleat...
Hilary P. Stevenson9
Estimated H-index: 9
(University of Pittsburgh),
Alexander M. Makhov17
Estimated H-index: 17
(University of Pittsburgh)
+ 13 AuthorsTed M. Ross22
Estimated H-index: 22
The current practice for identifying crystal hits for X-ray crystallography relies on optical microscopy techniques that are limited to detecting crystals no smaller than 5 μm. Because of these limitations, nanometer-sized protein crystals cannot be distinguished from common amorphous precipitates, and therefore go unnoticed during screening. These crystals would be ideal candidates for further optimization or for femtosecond X-ray protein nanocrystallography. The latter technique offers the pos...
Giuseppe Vitiello16
Estimated H-index: 16
(University of Naples Federico II),
Gaetano Mangiapia18
Estimated H-index: 18
(University of Naples Federico II)
+ 5 AuthorsGerardino D’Errico11
Estimated H-index: 11
(University of Naples Federico II)
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Published on Dec 1, 2013in FEBS Journal4.74
Richard Giegé53
Estimated H-index: 53
(CNRS: Centre national de la recherche scientifique)
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Published on Aug 12, 2013in ACS Combinatorial Science3.20
Shane A. Seabrook13
Estimated H-index: 13
Janet Newman26
Estimated H-index: 26
We present a high-throughput approach to help define experimental formulations that enhance protein stability, which is based on differential scanning fluorimetry (DSF). The method involves defining the thermal stability of a protein against a screen of 13 buffer systems, systematically sampling pH from 5.0 to 9.0 at high and low salt concentrations, using both redundancy and extensive controls to make the method robust. The screen allows rapid determination of a suitable base formulation for pr...
Published on Jun 1, 2013in Science China-chemistry6.08
Wei Wang1
Estimated H-index: 1
(SWU: Southwest University),
Chun Liu1
Estimated H-index: 1
(SWU: Southwest University)
+ 1 AuthorsChengZhi Huang5
Estimated H-index: 5
(SWU: Southwest University)
With the development of nanosciences, both localized surface plasmon resonance light scattering (LSPR-LS) and dynamic light scattering (DLS) techniques have been widely used for quantitative purposes with high sensitivity. In this contribution, we make a comparison of the two light scattering techniques by employing gold nanoparticles (AuNPs) aggregation induced by mercuric ions. It was found that citrate-stabilized AuNPs got aggregated in aqueous medium in the presence of mercuric ions through ...
Published on Sep 20, 2012
Obtaining X-ray suitable crystals is to date the rate limiting step to solve the structure of biological macromolecules such as proteins at atomic resolution. Those Structures are required for the design of novel drugs and to understand the way biological systems work. Rationalization of crystallization by biophysical methods is a promising way to accelerate this process. Here Dynamic Light Scattering (DLS) was applied in order to develop novel methods for the rationalization of crystallization ...
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