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    17 results match your criteria Acta crystallographica. Section F Structural biology and crystallization communications[Journal]

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    Preliminary crystallographic analysis of RraB from Escherichia coli.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2013 Nov 30;69(Pt 11):1268-71. Epub 2013 Oct 30.
    School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
    RraB, an inhibitor of the essential endoribonuclease RNE in Escherichia coli, is essential in regulating the abundance of RNA by directly interacting with RNE. In this study, RraB from E. coli was cloned, expressed, purified and crystallized. Read More

    Crystallization reports are the backbone of Acta Cryst. F, but do they have any spine?
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2013 Jul 30;69(Pt 7):712-8. Epub 2013 Jun 30.
    Materials, Science and Engineering Division, CSIRO, 343 Royal Parade, Parkville, VIC 3052, Australia.
    Crystallization of macromolecules is famously difficult. By knowing what has worked for others, researchers can ease the process, both in the case where the protein has already been crystallized and in the situation where more general guidelines are needed. The 264 crystallization communications published in Acta Crystallographica Section F in 2012 have been reviewed, and from this analysis some information about trends in crystallization has been gleaned. Read More

    Structural genomics of infectious disease drug targets: the SSGCID.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2011 Sep 13;67(Pt 9):979-84. Epub 2011 Aug 13.
    Seattle Structural Genomics Center for Infectious Disease, USA.
    The Seattle Structural Genomics Center for Infectious Disease (SSGCID) is a consortium of researchers at Seattle BioMed, Emerald BioStructures, the University of Washington and Pacific Northwest National Laboratory that was established to apply structural genomics approaches to drug targets from infectious disease organisms. The SSGCID is currently funded over a five-year period by the National Institute of Allergy and Infectious Diseases (NIAID) to determine the three-dimensional structures of 400 proteins from a variety of Category A, B and C pathogens. Target selection engages the infectious disease research and drug-therapy communities to identify drug targets, essential enzymes, virulence factors and vaccine candidates of biomedical relevance to combat infectious diseases. Read More

    Purification, crystallization and preliminary X-ray crystallographic analysis of a central domain of human splicing factor 1.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2011 Apr 25;67(Pt 4):486-90. Epub 2011 Mar 25.
    Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA.
    Pre-mRNA splicing is an essential source of genetic diversity in eukaryotic organisms. In the early stages of splicing, splicing factor 1 (SF1) recognizes the pre-mRNA splice site as a complex with its partner, U2 auxiliary factor 65 kDa subunit (U2AF(65)). A central `mystery' domain of SF1 (SF1md) lacks detectable homology with known structures, yet is the region of highest phylogenetic sequence conservation among SF1 homologues. Read More

    TOPSAN: use of a collaborative environment for annotating, analyzing and disseminating data on JCSG and PSI structures.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2010 Oct 30;66(Pt 10):1143-7. Epub 2010 Sep 30.
    Center for Research in Biological Systems, University of California, San Diego, La Jolla, California, USA.
    The NIH Protein Structure Initiative centers, such as the Joint Center for Structural Genomics (JCSG), have developed highly efficient technological platforms that are capable of experimentally determining the three-dimensional structures of hundreds of proteins per year. However, the overwhelming majority of the almost 5000 protein structures determined by these centers have yet to be described in the peer-reviewed literature. In a high-throughput structural genomics environment, the process of structure determination occurs independently of any associated experimental characterization of function, which creates a challenge for the annotation and analysis of structures and the publication of these results. Read More

    Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2009 Sep 20;65(Pt 9):862-5. Epub 2009 Aug 20.
    Synchrotron Radiation Research Section, MCL, National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439, USA.
    The crystal structure of the esterase EstA from the cold-adapted bacterium Pseudoalteromonas sp. 643A was determined in a covalently inhibited form at a resolution of 1.35 A. Read More

    Crystallization and preliminary X-ray diffraction of the DEAD-box protein Mss116p complexed with an RNA oligonucleotide and AMP-PNP.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2009 Aug 30;65(Pt 8):832-5. Epub 2009 Jul 30.
    Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, and Section of Molecular Genetics and Microbiology, School of Biological Sciences, University of Texas at Austin, Austin, TX 78712, USA.
    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/Delta598-664) were overproduced in Escherichia coli and purified to homogeneity. Mss116p exhibited low solubility in standard solutions (< or =1 mg ml(-1)), but its solubility could be increased by adding 50 mM L-arginine plus 50 mM L-glutamate and 50% glycerol to achieve concentrations of approximately 10 mg ml(-1). Read More

    Crystallization and preliminary crystallographic analysis of the complex of the second and third regulatory subunits of human Pol delta.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2008 Sep 20;64(Pt 9):822-4. Epub 2008 Aug 20.
    Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, 986805 Nebraska Medical Center, Omaha, NE 68198-7696, USA.
    Human DNA polymerase delta (Pol delta) consists of four subunits: p125, p50, p66 and p12. A heterodimer containing a His-tagged p50 subunit (p50) and a p50-interacting domain of the p66 subunit (p66(N)) was crystallized. The crystal was in the form of a prism with a rhombic cross-section and belonged to space group P2(1). Read More

    Cloning, purification and preliminary X-ray analysis of the C-terminal domain of Helicobacter pylori MotB.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2008 Apr 21;64(Pt 4):277-80. Epub 2008 Mar 21.
    Manchester Interdisciplinary Biocentre, Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester M1 7DN, England.
    The C-terminal domain of MotB (MotB-C) contains a putative peptidoglycan-binding motif and is believed to anchor the MotA/MotB stator unit of the bacterial flagellar motor to the cell wall. Crystals of Helicobacter pylori MotB-C (138 amino-acid residues) were obtained by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant. These crystals belong to space group P2(1), with unit-cell parameters a = 50. Read More

    Expression, purification and preliminary X-ray characterization of DL-2-haloacid dehalogenase from Methylobacterium sp. CPA1.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2007 Jul 15;63(Pt 7):586-9. Epub 2007 Jun 15.
    Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
    DL-2-Haloacid dehalogenase from Methylobacterium sp. CPA1 (DL-DEX Mb) is a unique enzyme that catalyzes the dehalogenation reaction without the formation of an ester intermediate. A recombinant form of DL-DEX Mb has been expressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. Read More

    Cloning, expression, purification, crystallization and preliminary crystallographic analysis of pseudo death-effector domain of HIPPI, a molecular partner of Huntingtin-interacting protein HIP-1.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2006 Dec 30;62(Pt 12):1247-50. Epub 2006 Nov 30.
    Structural Genomics Section, Saha Institute of Nuclear Physics, 1/AF Bidhan Nagar, Kolkata 700064, India.
    The formation of a heterodimer between Huntingtin-interacting protein-1 (HIP-1) and its novel partner HIPPI (HIP-1 protein interactor) through their pseudo death-effector domains (pDEDs) is a key step that recruits caspase-8 and initiates apoptosis. This could be one of the pathways by which apoptosis is increased in Huntington's disease (HD). A construct consisting of the pDED of HIPPI has been cloned and overexpressed as 6NH-tagged protein and purified by Ni-NTA affinity chromatography. Read More

    Expression, limited proteolysis and preliminary crystallographic analysis of IpaD, a component of the Shigella flexneri type III secretion system.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2006 Sep 11;62(Pt 9):865-8. Epub 2006 Aug 11.
    Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, England.
    IpaD, the putative needle-tip protein of the Shigella flexneri type III secretion system, has been overexpressed and purified. Crystals were grown of the native protein in space group P2(1)2(1)2(1), with unit-cell parameters a = 55.9, b = 100. Read More

    Expression, purification, crystallization and preliminary crystallographic analysis of MxiH, a subunit of the Shigella flexneri type III secretion system needle.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2006 Mar 28;62(Pt 3):302-5. Epub 2006 Feb 28.
    Department of Biochemistry, University of Oxford, England.
    A monodisperse truncation mutant of MxiH, the subunit of the needle from the Shigella flexneri type III secretion system (TTSS), has been overexpressed and purified. Crystals were grown of native and selenomethionine-labelled MxiH(CDelta5) and diffraction data were collected to 1.9 A resolution. Read More

    Crystallization and preliminary X-ray analysis of methylthioribose-1-phosphate isomerase from Bacillus subtilis.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 2005 Jun 1;61(Pt 6):595-8. Epub 2005 Jun 1.
    Department of Materials Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan.
    Methylthioribose-1-phosphate isomerase (MtnA) from Bacillus subtilis, the first enzyme in the downstream section of the methionine-salvage pathway, was crystallized using the sitting-drop vapour-diffusion method. Crystals grew using ammonium sulfate as the precipitant at 293 K. They diffracted to 2. Read More

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