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Feigelson, Robert S.

Publications and source records attributed to Feigelson, Robert S..

Investigation of the Crystal Growth of Dielectric Materials by the Bridgman Technique Using Vibrational Control

The principal goal of this ground-based program, which started on February 1, 1998 and concluded on April 30, 2002, was to investigate the influence of low frequency vibrations on the fluid flow and quality of dielectric oxide crystals grown by the vertical Bridgman method. This experimental program was a collaborative effort between Stanford University and the General Physics Institute of the Russian Academy of Sciences in Moscow, and included a strong emphasis on both physical modeling and the growth of some technologically important materials. Additionally it was carried out initially in collaboration with the theoretical and numerical investigations of A.Fedoseyev and I.Alexander (ongoing in another NASA sponsored program). This latter program involved a study of vibro-convective buoyancy-driven flows in cylindrical configurations with the expectation of being able to use vibrational flows to control buoyancy driven fluid transport to off-set the effect of "g-jitter" during microgravity Bridgman crystal growth. These two programs taken together, were designed to lead to a new parametric control variable which can be used to either suppress or control convection, and thereby heat and mass transport during Bridgman crystal growth. It was expected to be effective in either a terrestrial or space environment.

Feigelson, Robert S.

Laser Scattering Tomography for the Study of Defects in Protein Crystals

The goal of this research is to explore the application of the non-destructive technique of Laser Scattering Tomography (LST) to study the defects in protein crystals and relate them to the x-ray diffraction performance of the crystals. LST has been used successfully for the study of defects in inorganic crystals and. in the case of lysozyme, for protein crystals.

Feigelson, Robert S.

Protein crystal growth in low gravity

This research involved (1) using the Atomic Force Microscope (AFM) in a study on the growth of lysozyme crystals and (2) refinement of the design of the Thermonucleator which controls the supersaturation required for the nucleation and growth of protein crystals separately. AFM studies of the (110) tetragonal face confirmed that lysozyme crystals grow by step propagation. There appears to be very little step pile up in the growth regimes which we studied. The step height was measured at = 54A which was equal to the (110) interpane spacing. The AFM images showed areas of step retardation and the formation of pits. These defects ranged in size from 0.1 to 0.4 mu. The source of these defects was not determined. The redesign of the Thermonucleator produced an instrument based on thermoelectric technology which is both easier to use and more amenable to use in a mu g environment. The use of thermoelectric technology resulted in a considerable size reduction which will allow for the design of a multi-unit growth apparatus. The performance of the new apparatus was demonstrated to be the same as the original design.

Feigelson, Robert S.

Thermonucleator

Thermonucleator controls nucleation in selected region of crystallizing solution by varying local temperature and local supersaturation. Apparatus potentially offers better control of crystallization process in aqueous solution than use of stream of cold gas to induce nucleation by cooling part of bottom of crucible containing hot solution.

Demattei, Robert C.

Protein crystal growth in low gravity

This Final Technical Report for NASA Grant NAG8-774 covers the period from April 27, 1989 through December 31, 1992. It covers five main topics: fluid flow studies, the influence of growth conditions on the morphology of isocitrate lyase crystals, control of nucleation, the growth of lysozyme by the temperature gradient method and graphoepitaxy of protein crystals. The section on fluid flow discusses the limits of detectability in the Schlieren imaging of fluid flows around protein crystals. The isocitrate lyase study compares crystals grown terrestrially under a variety of conditions with those grown in space. The controlling factor governing the morphology of the crystals is the supersaturation. The lack of flow in the interface between the drop and the atmosphere in microgravity causes protein precipitation in the boundary layer and a lowering of the supersaturation in the drop. This lowered supersaturation leads to improved crystal morphology. Preliminary experiments with lysozyme indicated that localized temperature gradients could be used to nucleate crystals in a controlled manner. An apparatus (thermonucleator) was designed to study the controlled nucleation of protein crystals. This apparatus has been used to nucleate crystals of materials with both normal (ice-water, Rochelle salt and lysozyme) and retrograde (horse serum albumin and alpha chymotrypsinogen A) solubility. These studies have lead to the design of an new apparatus that small and more compatible with use in microgravity. Lysozyme crystals were grown by transporting nutrient from a source (lysozyme powder) to the crystal in a temperature gradient. The influence of path length and cross section on the growth rate was demonstrated. This technique can be combined with the thermonucleator to control both nucleation and growth. Graphoepitaxy utilizes a patterned substrate to orient growing crystals. In this study, silicon substrates with 10 micron grooves were used to grow crystals of catalase, lysozyme and canavalin. In all cases, the crystals grew oriented to the substrate. The supersaturation needed for nucleation and growth was lower on the patterned substrates. In some cases, isolated, large crystals were grown.

Feigelson, Robert S.

Factors affecting the morphology of isocitrate lyase crystals

Isocitrate lyase crystals have been grown by the hanging drop vapor equilibration method in both 1-g and microgravity and by vapor equilibrium in small capillaries. The crystal morphologies obtained have ranged from dendritic to 'octagonal' prisms. Theoretical evaporation models have been applied to these growth regimes. The results of these analyses along with other experimental results, indicate the factors which must be controlled to produce good growth morphologies.

Demattei, Robert C.

Protein crystal growth in low gravity

A study is presented of the crystallization of isocitrate lyase (ICL) and the influence of the lack of thermal solutal convection in microgravity on the morphology of ICL crystals is discussed. The latest results of studies with thermonucleation are presented. These include the nucleation of a protein with retrograde solubility and an unknown solubility curve. A new design for a more microgravity compatible thermonuclear is presented.

Feigelson, Robert S.

Protein crystal growth in low gravity

The objective of this research is to study the effect of low gravity on the growth of protein crystals and those parameters which will affect growth and crystal quality. The application of graphoepitaxy (artificial epitaxy) to proteins is detailed. The development of a method for the control of nucleation is discussed. The factor affecting the morphology of isocitrate lyase crystals is presented.

Feigelson, Robert S.

Protein crystal growth in low gravity

The effect of low gravity on the growth of protein crystals and those parameters which will affect growth and crystal quality was studied. The proper design of the flight hardware and experimental protocols are highly dependent on understanding the factors which influence the nucleation and growth of crystals of biological macromolecules. Thus, those factors are investigated and the body of knowledge which has been built up for small molecule crystallization. These data also provide a basis of comparison for the results obtained from low-g experiments. The flows around growing crystals are detailed. The preliminary study of the growth of isocitrate lyase, the crystal morphologies found and the preliminary x ray results are discussed. The design of two apparatus for protein crystal growth by temperature control are presented along with preliminary results.

Feigelson, Robert S.

Protein crystal growth in low gravity

The mechanisms involved in protein crystallization and those parameters which influence the growth process and crystalline perfection were studied. The analysis of the flows around growing crystals is detailed. The preliminary study of the growth of isocitrate lyase and the crystal morphologies found are discussed. Preliminary results of controlled nucleation studies are presented.

Feigelson, Robert S.

Making Single Crystals of B4C

Crystals precipitate from solution in copper. Well-defined single crystals of boron carbide (B4C) grown by slowly cooling melts containing B4C and copper. Forms on surface and in interior of melt.

Feigelson, Robert S.

Protein crystal growth in low gravity

The solubility and growth of the protein canavalin, and the application of the schlieren technique to study fluid flow in protein crystal growth systems were investigated. These studies have resulted in the proposal of a model to describe protein crystal growth and the preliminary plans for a long-term space flight experiment. Canavalin, which may be crystallized from a basic solution by the addition of hydrogen (H+) ions, was shown to have normal solubility characteristics over the range of temperatures (5 to 25 C) and pH (5 to 7.5) studies. The solubility data combined with growth rate data gathered from the seeded growth of canavalin crystals indicated that the growth rate limiting step is a screw dislocation mechanism. A schlieren apparatus was constructed and flow patterns were observed in Rochelle salt (sodium potassium tartrate), lysozyme, and canavalin. The critical parameters were identified as the change in density with concentration (dp/dc) and the change in index of refraction with concentration (dn/dc). Some of these values were measured for the materials listed. The data for lyrozyme showed non-linearities in plots of optical properties and density vs. concentration. In conjunction with with W. A. Tiller, a model based on colloid stability theory was proposed to describe protein crystallization. The model was used to explain observations made by ourselves and others. The results of this research has lead to the development for a preliminary design for a long-term, low-g experiment. The proposed apparatus is univeral and capable of operation under microprocessor control.

Feigelson, Robert S.

Protein crystal growth in low gravity

The solubility and growth mechanism of canavalin were studied, and the applicability of the Schlieren technique to protein crystal growth was investigated. Canavalin which may be crystallized from a basic solution by the addition of hydrogen (H+) ions was shown to have normal solubility characteristics over the range of temperatures (5 to 25 C) and pH (5 to 7.5) studied. The solubility data combined with growth rate data gathered from the seeded growth of canavalin crystals indicated that the growth mechanism at high supersaturation ratios (>1.28) is screw dislocation like. A Schlieren apparatus was constructed and flow patterns were observed in Rochelle salt (sodium potassium tartrate), lysozyme, and canavalin. The critical parameters were identified as the change in density with concentration (dp/dc) and the change in index of refraction with concentration (dn/dc). Some of these values were measured for the materials listed.

Feigelson, Robert S.

Infrared fiber optic materials

The development of IR fiber optics for use in astronomical and other space applications is summarized. Candidate materials were sought for use in the 1 to 200 micron and the 200 to 1000 micron wavelength range. Synthesis and optical characterization were carried out on several of these materials in bulk form. And the fabrication of a few materials in single crystal fiber optic form were studied.

Feigelson, Robert S.