Home  About us  Contact
 

Preliminary X-ray Diffraction (preliminary + x-ray_diffraction)

Distribution by Scientific Domains
Chemistry100%

Terms modified by Preliminary X-ray Diffraction

  • preliminary x-ray diffraction analysis
  • preliminary x-ray diffraction data
    		•
  • preliminary x-ray diffraction studies
  • preliminary x-ray diffraction study
    		•

    Selected Abstracts

    Purification, crystallization and preliminary X-ray diffraction of a proteolytic fragment of PDK1 containing the pleckstrin homology domain

    ACTA CRYSTALLOGRAPHICA SECTION D, Issue 2 2004
    David Komander
    3-Phosphoinositide-dependent protein kinase-1 (PDK1) is a Ser/Thr kinase with an essential role in insulin and growth-factor signalling. PDK1 activity towards protein kinase B (PKB) is partially regulated by its pleckstrin homology (PH) domain, which preferentially binds to 3-phosphoinositides. However, the precise molecular mechanism of this regulation is not well understood. Here, the cloning, purification and crystallization of a 150-amino-acid C-terminal region of PDK1 containing the PH domain is reported. A crystal of the PDK1 PH domain grown in the presence of inositol 1,3,4,5-tetrakisphosphate and derivatized with AuCN diffracted to 1.5,Å at a synchrotron source. Diffraction data collected near the Au edge resulted in an anomalous Patterson map with a 30, peak. [source]

    Cloning, purification, crystallization and preliminary X-ray diffraction of the OleC protein from Stenotrophomonas maltophilia involved in head-to-head hydrocarbon biosynthesis

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2010
    Janice A. Frias
    OleC, a biosynthetic enzyme involved in microbial hydrocarbon biosynthesis, has been crystallized. Synchrotron X-ray diffraction data have been collected to 3.4,Å resolution. The crystals belonged to space group P3121 or P3221, with unit-cell parameters a = b = 98.8, c = 141.0,Å. [source]

    Crystallization and preliminary X-ray diffraction of chlorite dismutase from Dechloromonas aromatica RCB

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2009
    Brandon R. Goblirsch
    Chlorite dismutase from Dechloromonas aromatica RCB, a novel b -type hemoprotein that catalyzes O,O bond formation, has been crystallized. Synchrotron X-ray diffraction data have been collected to 3.0,Å resolution. The crystals belonged to space group P212121, with unit-cell parameters a = 122.7, b = 202.9, c = 247.1,Å. [source]

    Crystallization and preliminary X-ray diffraction of the DEAD-box protein Mss116p complexed with an RNA oligonucleotide and AMP-PNP

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2009
    Mark Del Campo
    The Saccharomyces cerevisiae DEAD-box protein Mss116p is a general RNA chaperone which functions in mitochondrial group I and group II intron splicing, translation and RNA-end processing. For crystallization trials, full-length Mss116p and a C-terminally truncated protein (Mss116p/,598,664) were overproduced in Escherichia coli and purified to homogeneity. Mss116p exhibited low solubility in standard solutions (,1,mg,ml,1), but its solubility could be increased by adding 50,mMl -arginine plus 50,mMl -glutamate and 50% glycerol to achieve concentrations of ,10,mg,ml,1. Initial crystals were obtained by the microbatch method in the presence of a U10 RNA oligonucleotide and the ATP analog AMP-PNP and were then improved by using seeding and sitting-drop vapor diffusion. A cryocooled crystal of Mss116p/,598,664 in complex with AMP-PNP and U10 belonged to space group P21212, with unit-cell parameters a = 88.54, b = 126.52, c = 55.52,Å, and diffracted X-rays to beyond 1.9,Å resolution using synchrotron radiation from sector 21 at the Advanced Photon Source. [source]

    Purification, crystallization and preliminary X-ray diffraction of wild-type and mutant recombinant human transforming growth factor ,-induced protein (TGFBIp)

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 3 2009
    Kasper Runager
    Transforming growth factor ,-induced protein (TGFBIp) has been linked to several corneal dystrophies as certain point mutations in the protein may give rise to a progressive accumulation of insoluble protein material in the human cornea. Little is known about the biological functions of this extracellular protein, which is expressed in various tissues throughout the human body. However, it has been found to interact with a number of extracellular matrix macromolecules such as collagens and proteoglycans. Structural information about TGFBIp might prove to be a valuable tool in the elucidation of its function and its role in corneal dystrophies caused by mutations in the TGFBI gene. A simple method for the purification of wild-type and mutant forms of recombinant human TGFBIp from human cells under native conditions is presented here. Moreover, the crystallization and preliminary X-ray analysis of TGFBIp are reported. [source]

    Expression, purification, crystallization and preliminary X-ray analysis of an NAD-dependent glyceraldehyde-3-phosphate dehydrogenase from Helicobacter pylori

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2008
    Paul R. Elliott
    Helicobacter pylori is a dangerous human pathogen that resides in the upper gastrointestinal tract. Little is known about its metabolism and with the onset of antibiotic resistance new treatments are required. In this study, the expression, purification, crystallization and preliminary X-ray diffraction of an NAD-dependent glyceraldehyde-3-phosphate dehydrogenase from H. pylori are reported. [source]

    Crystallization and preliminary X-ray diffraction of human interleukin-7 bound to unglycosylated and glycosylated forms of its ,-receptor

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 10 2007
    Joseph Wickham Jr
    The interleukin-7 (IL-7) signaling pathway plays an essential role in the development, proliferation and homeostasis of T and B cells in cell-mediated immunity. Understimulation and overstimulation of the IL-7 signaling pathway leads to severe combined immunodeficiency, autoimmune reactions, heart disease and cancers. Stimulation of the IL-7 pathway begins with IL-7 binding to its ,-receptor, IL-7R,. Protein crystals of unglycosylated and glycosylated complexes of human IL-7,IL-7R, extracellular domain (ECD) obtained using a surface entropy-reduction approach diffract to 2.7 and 3.0,Å, respectively. Anomalous dispersion methods will be used to solve the unglycosylated IL-7,IL-7R, ECD complex structure and this unglycosylated structure will then serve as a model in molecular-replacement attempts to solve the structure of the glycosylated IL-7,,-receptor complex. [source]

    Crystallization, preliminary X-ray diffraction and structure analysis of Thermotoga maritima mannitol dehydrogenase

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2007
    Jennifer Puttick
    Diffraction data have been collected from a crystal of Thermotoga maritima mannitol dehydrogenase at the Canadian Light Source. The crystal diffracted to 3.3,Å resolution and belongs to space group P212121, with unit-cell parameters a = 83.43, b = 120.61, c = 145.76,Å. The structure is likely to be solved by molecular replacement. [source]

    Purification, crystallization and preliminary X-ray diffraction of human S100A15

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 5 2006
    Karen M. Boeshans
    Human S100A15 is a novel member of the S100 family of EF-hand calcium-binding proteins and was recently identified in psoriasis, where it is significantly upregulated in lesional skin. The protein is implicated as an effector in calcium-mediated signal transduction pathways. Although its biological function is unclear, the association of the 11.2,kDa S100A15 with psoriasis suggests that it contributes to the pathogenesis of the disease and could provide a molecular target for therapy. To provide insight into the function of S100A15, the protein was crystallized to visualize its structure and to further the understanding of how the many similar calcium-binding mediator proteins in the cell distinguish their cognate target molecules. The S100A15 protein has been cloned, expressed and purified to homogeneity and produced two crystal forms. Crystals of form I are triclinic, with unit-cell parameters a = 33.5, b = 44.3, c = 44.8,Å, , = 71.2, , = 68.1, , = 67.8° and an estimated two molecules in the asymmetric unit, and diffract to 1.7,Å resolution. Crystals of form II are monoclinic, with unit-cell parameters a = 82.1, b = 33.6, c = 52.2,Å, , = 128.2° and an estimated one molecule in the asymmetric unit, and diffract to 2.0,Å resolution. This structural analysis of the human S100A15 will further aid in the phylogenic comparison between the other members of the S100 protein family, especially the highly homologous paralog S100A7. [source]

    Incorporation of a disaccharide nucleoside into the backbone of double-stranded DNA: crystallization and preliminary X-ray diffraction

    ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 10 2005
    Kristof Van Hecke
    Incorporation of a disaccharide nucleoside into double-stranded DNA can be considered as a chemical (non-enzymatic) alternative for site-specific cleavage of DNA. Crystals of the sequence d(CGCGAATT*CGCG), where * is an incorporated ribose, were obtained by hanging-drop vapour diffusion and diffracted to 2.6,Å. The crystals belong to the orthorhombic space group P2221, with unit-cell parameters a = 41.52, b = 57.63, c = 81.39,Å, indicating a new crystal packing motif for an oligonucleotide dodecamer sequence. [source]