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  • MATERIALS PROCESSING  (7)
  • Life Sciences (General)  (1)
  • 1
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    Protein crystal growth in microgravity (1989)
    In:  CASI
    Details
    Publication Date: 2006-06-11
    Description: Major advances have been made in several of the experimental aspects of protein crystallography, leaving protein crystallization as one of the few remaining bottlenecks. As a result, it has become important that the science of protein crystal growth is better understood and that improved methods for protein crystallization are developed. Preliminary experiments with both small molecules and proteins indicate that microgravity may beneficially affect crystal growth. For this reason, a series of protein crystal growth experiments using the Space Shuttle was initiated. The preliminary space experiments were used to evolve prototype hardware that will form the basis for a more advanced system that can be used to evaluate effects of gravity on protein crystal growth. Various optical techniques are being utilized to monitor the crystal growth process from the incipient or nucleation stage and throughout the growth phase. The eventual goal of these studies is to develop a system which utilizes optical monitoring for dynamic control of the crystallization process.
    Keywords: MATERIALS PROCESSING
    Type: NASA, Lewis Research Center, NASA Laser Light Scattering Advanced Technology Development Workshop, 1988; p 235-256
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  • 2
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    Protein crystal growth results from the United States Microgravity Laboratory-1 mission (1994)
    In:  CASI
    Details
    Publication Date: 2013-08-31
    Description: Protein crystal growth experiments have been performed by this laboratory on 18 Space Shuttle missions since April, 1985. In addition, a number of microgravity experiments also have been performed and reported by other investigators. These Space Shuttle missions have been used to grow crystals of a variety of proteins using vapor diffusion, liquid diffusion, and temperature-induced crystallization techniques. The United States Microgravity Laboratory - 1 mission (USML-1, June 25 - July 9, 1992) was a Spacelab mission dedicated to experiments involved in materials processing. New protein crystal growth hardware was developed to allow in orbit examination of initial crystal growth results, the knowledge from which was used on subsequent days to prepare new crystal growth experiments. In addition, new seeding hardware and techniques were tested as well as techniques that would prepare crystals for analysis by x-ray diffraction, a capability projected for the planned Space Station. Hardware that was specifically developed for the USML-1 mission will be discussed along with the experimental results from this mission.
    Keywords: MATERIALS PROCESSING
    Type: NASA. Marshall Space Flight Center, Joint Launch + One Year Science Review of USML-1 and USMP-1 with the Microgravity Measurement Group; p 409-445
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  • 3
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    Protein crystal growth in microgravity (1991)
    In:  Other Sources
    Details
    Publication Date: 2019-07-13
    Description: A series of protein-crystal growth experiments were performed on Space Shuttle flight STS-26 in September 1988 and STS-29 in March 1989. These proteins had been studied extensively in crystal-growth experiments on earth prior to the microgravity experiments. For those proteins which produced crystals of adequate size, 3D intensity data sets with electronic area detector systems were collected. Comparisons show that the microgravity-grown crystals of these proteins are larger, display more uniform morphologies, and yield diffraction data to significantly higher resolutions. Analyses of the 3D data sets indicate that the space-grown crystals are more highly ordered at the molecular level than their earth-grown counterparts.
    Keywords: MATERIALS PROCESSING
    Type: AIAA/IKI Microgravity Science Symposium; May 13, 1991 - May 17, 1991; Moscow; USSR
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  • 4
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    Protein crystallization aboard the Space Shuttle and the Mir space station (1993)
    In:  Other Sources
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    Publication Date: 2019-07-13
    Description: Two different protein crystallizations, namely ,the free Fab fragment of the Je142 monoclonal antibody and the complex of Fab fragment/HPr with antigen, were performed aboard the Discovery Space Shuttle flights and the Mir space station, respectively. Medium sized crystals of the Je142 Fab fragment were obtained. The Je142 Fab fragment/Hpr complex produced two medium-sized crystals after two months aboard the Mir space station. Microgravity was found to eliminate the tendency of these crystals to form clusters.
    Keywords: MATERIALS PROCESSING
    Type: AIAA PAPER 93-0718 , AIAA, Aerospace Sciences Meeting and Exhibit; Jan 11, 1993 - Jan 14, 1993; Reno, NV; United States|; 4 p.
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  • 5
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    Protein crystal growth in microgravity (1989)
    In:  Other Sources
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    Publication Date: 2019-07-12
    Description: The crystals of most proteins or other biological macromolecules are poorly ordered and diffract to lower resolutions than those observed for most crystals of simple organic and inorganic compounds. Crystallization in the microgravity environment of space may improve crystal quality by eliminating convection effects near growing crystal surfaces. A series of 11 different protein crystal growth experiments was performed on U.S. Space Shuttle flight STS-26 in September 1988. The microgravity-grown crystals of gamma-interferon D1, porcine elastase, and isocitrate lyase are larger, display more uniform morphologies, and yield diffraction data to significantly higher resolutions than the best crystals of these proteins grown on earth.
    Keywords: MATERIALS PROCESSING
    Type: Science (ISSN 0036-8075); 246; 651-654
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  • 6
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    Dynamically controlled crystal growth system (2002)
    In:  CASI
    Details
    Publication Date: 2019-07-12
    Description: Crystal growth can be initiated and controlled by dynamically controlled vapor diffusion or temperature change. In one aspect, the present invention uses a precisely controlled vapor diffusion approach to monitor and control protein crystal growth. The system utilizes a humidity sensor and various interfaces under computer control to effect virtually any evaporation rate from a number of different growth solutions simultaneously by means of an evaporative gas flow. A static laser light scattering sensor can be used to detect aggregation events and trigger a change in the evaporation rate for a growth solution. A control/follower configuration can be used to actively monitor one chamber and accurately control replicate chambers relative to the control chamber. In a second aspect, the invention exploits the varying solubility of proteins versus temperature to control the growth of protein crystals. This system contains miniature thermoelectric devices under microcomputer control that change temperature as needed to grow crystals of a given protein. Complex temperature ramps are possible using this approach. A static laser light scattering probe also can be used in this system as a non-invasive probe for detection of aggregation events. The automated dynamic control system provides systematic and predictable responses with regard to crystal size. These systems can be used for microgravity crystallization projects, for example in a space shuttle, and for crystallization work under terrestial conditions. The present invention is particularly useful for macromolecular crystallization, e.g. for proteins, polypeptides, nucleic acids, viruses and virus particles.
    Keywords: Life Sciences (General)
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  • 7
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    Protein crystal growth in space (1991)
    In:  Other Sources
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    Publication Date: 2019-08-28
    Description: Studies of protein crystal growth in the microgravity environment in space are described with special attention given to the crystal growth facilities and the techniques used in Space Shuttle experiments. The properties of large space-grown crystals of gamma interferon, elastase, lathyros ochrus lectin I, and few other proteins grown on various STS flights are described. A comparison of the microgravity-grown crystals with the bast earth-grown crystals demonstrated that the space-grown crystals are more highly ordered at the molecular level than their earth-grown counterparts. When crystallization conditions were optimized, the microgravity-grown protein crystals were larger, displayed more uniform morphologies, and yielded diffraction data to significantly higher resolution than their earth-grown counterparts.
    Keywords: MATERIALS PROCESSING
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  • 8
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    Experimental and theoretical analysis of the rate of solvent equilibration in the hanging drop method of protein crystal growth (1988)
    In:  Other Sources
    Details
    Publication Date: 2019-07-12
    Description: The principles of the hanging-drop method of crystal growth are discussed, and the rate of water evaporation in a water droplet (containing protein, buffer, and a precipitating agent) suspended above a well containing a double concentration of precipitating agent is investigated theoretically. It is shown that, on earth, the rate of evaporation may be determined from diffusion theory and the colligative properties of solutions. The parameters affecting the rate of evaporation include the temperature, the vapor pressure of water, the ionization constant of the salt, the volume of the drop, the contact angle between the droplet and the coverslip, the number of moles of salt in the droplet, the number of moles of water and salt in the well, the molar volumes of water and salt, the distance from the droplet to the well, and the coefficient of diffusion of water vapor through air. To test the theoretical equations, hanging-drop experiments were conducted using various reagent concentrations in 25-microliter droplets and measuring the evaporation times at 4 C and 25 C. The results showed good agreement with the theory.
    Keywords: MATERIALS PROCESSING
    Type: Journal of Crystal Growth (ISSN 0022-0248); 90; 1-3
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