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  • 1
    Electronic Resource
    Electronic Resource
    New Crystallization Systems Envisioned for Microgravity Studies (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 31 (1998), S. 515-522 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Laboratory-based systems have been constructed to demonstrate two methods which will allow for dynamic control of protein-crystal growth. The technologies developed in these systems will be incorporated into future flight hardware for use in microgravity studies. The first method uses a precisely controlled vapor-diffusion approach to monitor and control protein crystal growth. This approach utilizes a humidity sensor and various interfaces under computer control to effect virtually any evaporation rate from up to 40 different growth solutions simultaneously. 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. The second method exploits the varying solubility of proteins versus temperature to control the growth of protein crystals. This approach utilizes miniature thermoelectric devices under microcomputer control which 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 is also included in this system as a noninvasive probe for detection of aggregation events. The systems constructed demonstrate significant advances in the ability of researchers to gain control of the protein-crystal growth process and will provide tremendous opportunities for microgravity research.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889897010571
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary structure determination of porcine aldehyde reductase from two crystal forms (1993)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 49 (1993), S. 490-496 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Aldehyde reductase from porcine kidney has been crystallized from buffered ammonium sulfate solutions. Two crystal forms are monoclinic, space group P21, with a = 56.2, b = 98.1, c = 73.2 Å, β = 112.5° and a = 92.4, b = 62.1, c = 59.0 Å, β = 94.6°. A third crystal form is hexagonal with a = b = 166.0, c = 66.0 Å, α = β = 90.0° and γ = 120.0°. Molecular-replacement structure solutions have been successfully obtained for the two monoclinic crystal forms. The crystallographic R factor at 8–2.8 Å resolution for the two monoclinic crystal forms is currently 0.23 and 0.25, respectively. There are two molecules per asymmetric unit related by a non-crystallographic twofold axis. The aldehyde reductase models are supported by the arrangement of the molecules in their respective unit cells and by electron densities corresponding to amino-acid side chains not included in the search structures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444993004044
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  • 3
    Electronic Resource
    Electronic Resource
    Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 859-868 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structures of porcine and human aldehyde reductase, an enzyme implicated in complications of diabetes, have been determined by X-ray diffraction methods. The crystallographic R factor for the refined porcine aldehyde reductase model is 0.19 at 2.8 Å resolution. There are two molecules in the asymmetric unit related by a local non-crystallographic twofold axis. The human aldehyde reductase model has been refined to an R factor of 0.21 at 2.48 Å resolution. The amino-acid sequence of porcine aldehyde reductase revealed a remarkable homology with human aldehyde reductase. The coenzyme-binding site residues are conserved and adopt similar conformations in human and porcine aldehyde reductase apo-enzymes. The tertiary structures of aldhyde reductase and aldose reductase are similar and consist of a β/α-barrel, with the coenzyme-binding site located at the carboxy-terminus end of the strands of the barrel. The crystal structure of porcine and human aldehyde reductase should allow in vitro mutagenesis to elucidate the mechanism of action for this enzyme and facilitate the effective design of specific inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994005275
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  • 4
    Electronic Resource
    Electronic Resource
    Preface (1995)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 405-406 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444995004045
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  • 5
    Electronic Resource
    Electronic Resource
    Polarized Raman Spectroscopic Studies of Tetragonal Lysozyme Single Crystals (1998)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 54 (1998), S. 1216-1229 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Polarized Raman spectra have been obtained for tetragonal lysozyme single crystals of different relative quality. The Raman band at 507 cm−1, which corresponds to the totally symmetric stretch vibration of the gauche-gauche-gauche (ggg) disulfide bridges of the protein, has been shown to possess different polarization characteristics compared with the gauche-gauche-trans (ggt) disulfide bridge band at 528 cm−1. The relative intensities of the ggg and ggt bands in the polarized Raman spectra have been numerically estimated for a number of tetragonal lysozyme single crystals, the X-ray diffraction data of which are available from the Protein Data Bank. On the basis of comparison between the experimental and calculated polarization characteristics of the disulfide Raman lines, the following main conclusions have been drawn. The orientation of the protein molecules correlates with the average orientation of their ggg disulfide bridges. This in turn can be described by the ρggg value which reflects the average orientation of the S—S bonds with respect to the Z crystallographic axis and can be determined from polarized Raman spectra. Crystals of better quality are characterized by a better alignment of the protein molecules with respect to the Z axis, a smaller perturbation of the protein molecules in the crystal lattice and a somewhat higher interlattice water content.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998001486
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  • 6
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary structure of porcine aldehyde reductase–NADPH binary complex (1995)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 605-608 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Porcine aldehyde reductase–NADPH binary complex has been crystallized from a buffered ammonium sulfate solution. The crystal form is hexagonal, space group P6522, with a = b = 67.2, c = 243.7 Å, α = β = 90.0 and γ = 120.0°. A molecular-replacement structure solution has been successfully obtained by using the refined structure of the apoenzyme as the search model. The crystallographic R-factor is currently equal to 0.24 after energy minimization using data between 8 and 3.0 Å resolution. The aldehyde reductase–NADPH complex model is supported by electron density corresponding to NADPH not included in the search model. The tertiary structure of aldehyde reductase consists of a β/α-barrel with the coenzyme-binding site located at the carboxy-terminal end of the strands of the barrel. The structure of aldehyde reductase–NADPH binary complex will help clarify the mechanism of action for this enzyme and will lead to the development of pharmacologic agents to delay or prevent diabetic complications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994013995
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  • 7
    Electronic Resource
    Electronic Resource
    Crystallization of engineered Thermus flavus 5S rRNA under earth and microgravity conditions (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 498-500 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Thermus flavus 5S rRNA with a molecular weight of about 40 kDa was modified at the 5′ and 3′ ends. Crystals were obtained under earth and microgravity conditions. The best crystals were obtained during NASA space mission STS 94. For the first time, it was possible to collect a complete data set from 5S rRNA crystals to 7.8 Å resolution and to assign the space group as R32, with unit-cell parameters a = b = 110.3, c = 387.6 Å, α = β = 90, γ = 120°.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900001736
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  • 8
    Electronic Resource
    Electronic Resource
    Comparison of homology models with the experimental structure of a novel serine protease (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 889-899 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A model structure of the human complement enzyme factor D was built based on homology with related serine proteases. A molecular-replacement solution of the factor D crystal structure employing the homology model refined without manual intervention to an R factor of 0.249 with 2.4 Å native diffraction data. A multiple isomorphous replacement (MIR) electron-density map was subsequently produced, leading to a model refined at 2.0 Å resolution to an R factor of 0.188. A homology model built with commercial modeling software was subjected to the same procedure. Comparisons of the homology models with the final refined MIR structure are presented. Major discrepancies were found in critical active-site regions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994004907
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  • 9
    Electronic Resource
    Electronic Resource
    Preliminary crystallographic study on a low molecular weight form of bacterial plasminogen activator staphylokinase (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 480-481 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Staphylokinase, a 17 kDa protein, produced by certain strains of Staphylococcus aureus functions as a fibrin-specific plasminogen activator. During its interaction with plasminogen, staphylokinase is converted into a low molecular weight form by loss of ten amino-terminal residues. This low molecular weight form of recombinant staphylokinase has been crystallized using the hanging-drop vapor-diffusion technique with polyethylene glycol 4000 as precipitant. Crystals belong to the orthorhombic space group C2221 with unit-cell dimensions a = 43.78, b = 59.86 and c = 103.25 Å and one molecule in the asymmetric unit. These crystals diffract to about 2.4 Å resolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S090744499700084X
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  • 10
    Electronic Resource
    Electronic Resource
    Stacking patterns of thiopyrimidines: the crystal structure of 2-thiocytosine picrate (1977)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 33 (1977), S. 2611-2614 
    Details
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567740877009017
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