Determination of Local Refractive Index for Protein and Virus Crystals in Solution by Mach-Zehnder Interferometry

Cole, Tammy C.; Kathman, Alan D.; Koszelak, Stanley; McPherson, Alexander

doi:10.1006/abio.1995.1507

Cited by 28 publications

(16 citation statements)

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“…The only system specifically designed for that purpose, the Observable Protein Crystal Growth Apparatus (OPCGA) 81 though fully constructed and tested, failed to fly as a consequence of the Columbia Space Shuttle disaster. That system contained two sophisticated, solid optics Mach–Zehnder interferometers 82 as well as polarized light video microscopy (Figure 18). Following that misfortune, most microgravity science in low Earth orbit was abandoned for a significant time.…”

Section: Initial Results (Proof Of Concept)mentioning

confidence: 99%

Microgravity protein crystallization

McPherson

DeLucas

2015

npj Microgravity

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Over the past 20 years a variety of technological advances in X-ray crystallography have shortened the time required to determine the structures of large macromolecules (i.e., proteins and nucleic acids) from several years to several weeks or days. However, one of the remaining challenges is the ability to produce diffraction-quality crystals suitable for a detailed structural analysis. Although the development of automated crystallization systems combined with protein engineering (site-directed mutagenesis to enhance protein solubility and crystallization) have improved crystallization success rates, there remain hundreds of proteins that either cannot be crystallized or yield crystals of insufficient quality to support X-ray structure determination. In an attempt to address this bottleneck, an international group of scientists has explored use of a microgravity environment to crystallize macromolecules. This paper summarizes the history of this international initiative along with a description of some of the flight hardware systems and crystallization results.

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Section: Initial Results (Proof Of Concept)mentioning

confidence: 99%

Microgravity protein crystallization

McPherson

DeLucas

2015

npj Microgravity

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“…They usually exploit effects such as fluorescence emission and refractive index changes to detect the presence of specific substances [6][7][8] and offer unique advantages like immunity to electromagnetic interference, high sensitivity, and low price. Many types of integrated optical sensors have been developed like those based on Mach-Zehnder interferometers or waveguide bend loss [9][10][11][12]. The most promising are the integrated Mach-Zehnder interferometers, where the refractive index change of the substance placed on the sensor arm induces an optical path difference between the lightwaves propagating in the sensor and reference arms, respectively.…”

Section: Introductionmentioning

confidence: 99%

The Odorant-Binding Protein from Canis familiaris: Purification, Characterization and New Perspectives in Biohazard Assessment

D’Auria

Staiano²,

Varriale³

et al. 2006

PPL

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“…A core dielectric constant of 1.85 was determined from experimental data on the effective refractive index of the virus core. 48,49 The plasmon resonance calculated for the virus core is narrower than the measured nanoshell plasmon. This can be attributed to the rough and uneven shell structure discussed in the previous section.…”

Section: Theoretical Modeling Of the CIV Nanoshell Plasmonmentioning

confidence: 93%

Bio-scaffolds for ordered nanostructures and metallodielectric nanoparticles

et al. 2005

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The use of virus nanoparticles, specifically Chilo and Wiseana Invertebrate Iridovirus, as building blocks for iridescent nanoparticle assemblies and core substrates in the fabrication of metallodielectric nanostructures is discussed. Virus particles are assembled in vitro, yielding films and monoliths with optical iridescence arising from multiple Bragg scattering from close packed crystalline structures of the iridovirus. Bulk viral assemblies are prepared by centrifugation followed by the addition of glutaraldehyde, a cross-linking agent. Long range assemblies were prepared by employing a cell design that forced virus assembly within a confined geometry followed by cross-linking. In addition to these assemblies core-shell particles were created from the same virus. A gold shell is assembled around the viral core by attaching small gold nanoparticles to the virus surface by means of the inherent chemical functionality found within the protein cage structure of the viral capsid. These gold nanoparticles act as nucleation sites for electroless deposition of gold ions from solution. UV/Vis spectroscopy and electron microscopy, were used to verify the creation of the virus assemblages. The optical extinction spectra of the metallo-viral complex were compared to Mie scattering theory and found to be in quantitative agreement. These investigations demonstrate that direct harvesting of biological structures, rather than biochemical modification of protein sequences, is a viable route to create unique, optically active materials.

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Determination of Local Refractive Index for Protein and Virus Crystals in Solution by Mach-Zehnder Interferometry

Cited by 28 publications

References 0 publications

Microgravity protein crystallization

Microgravity protein crystallization

The Odorant-Binding Protein from Canis familiaris: Purification, Characterization and New Perspectives in Biohazard Assessment

Bio-scaffolds for ordered nanostructures and metallodielectric nanoparticles

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