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Sökning: WFRF:(Lohkamp B)

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  • Agirre, Jon, et al. (författare)
  • The CCP4 suite: integrative software for macromolecular crystallography
  • 2023
  • Ingår i: Acta Crystallographica Section D. - : INT UNION CRYSTALLOGRAPHY. - 2059-7983. ; 79, s. 449-461
  • Tidskriftsartikel (refereegranskat)abstract
    • The Collaborative Computational Project No. 4 (CCP4) is a UK-led international collective with a mission to develop, test, distribute and promote software for macromolecular crystallography. The CCP4 suite is a multiplatform collection of programs brought together by familiar execution routines, a set of common libraries and graphical interfaces. The CCP4 suite has experienced several considerable changes since its last reference article, involving new infrastructure, original programs and graphical interfaces. This article, which is intended as a general literature citation for the use of the CCP4 software suite in structure determination, will guide the reader through such transformations, offering a general overview of the new features and outlining future developments. As such, it aims to highlight the individual programs that comprise the suite and to provide the latest references to them for perusal by crystallographers around the world.
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4.
  • van Kuilenburg, A B P, et al. (författare)
  • Identification of two novel mutations C79X and R235Q in the dihydropyrimidine dehydrogenase gene in a patient presenting with hematuria
  • 2008
  • Ingår i: Nucleosides, Nucleotides & Nucleic Acids. - : Informa UK Limited. - 1525-7770 .- 1532-2335. ; 27:6-7, s. 809-815
  • Tidskriftsartikel (refereegranskat)abstract
    • A patient with hematuria was shown to have thymine-uraciluria. The dihydropyrimidine dehydrogenase (DPD) activity in peripheral blood mononuclear cells was 0.16 nmol/mg/h; controls: 9.9 +/- 2.8 nmol/mg/h. Analysis of DPYD showed that the patient was compound heterozygous for the novel mutations 237C > A (C79X) in exon 4 and 704G > A (R235Q) in exon 7. The nonsense mutation (C79X) leads to premature termination of translation and thus to a non-functional protein. Analysis of the crystal structure of pig DPD suggested that the R235Q mutation might interfere with the binding of FAD and the electron flow between the NADPH and the pyrimidine substrate site of DPD.
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  • Emsley, P, et al. (författare)
  • Features and development of Coot
  • 2010
  • Ingår i: Acta crystallographica. Section D, Biological crystallography. - 1399-0047. ; 66:Pt 4, s. 486-501
  • Tidskriftsartikel (refereegranskat)
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  • Lohkamp, B, et al. (författare)
  • Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum
  • 2006
  • Ingår i: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications. - : International Union of Crystallography (IUCr). - 2053-230X .- 1744-3091. ; 62:1, s. 36-38
  • Tidskriftsartikel (refereegranskat)abstract
    • Dihydropyrimidinase (EC 3.5.2.2) is the second enzyme in the reductive pyrimidine-degradation pathway and catalyses the hydrolysis of 5,6-dihydrouracil and 5,6-dihydrothymine to the corresponding N-carbamylated beta-amino acids. The recombinant enzyme from the slime mould Dictyostelium discoideum was overexpressed, purified and crystallized by the vapour-diffusion method. One crystal diffracted to better than 1.8 angstrom resolution on a synchrotron source and was shown to belong to space group I222, with unit-cell parameters a = 84.6, b = 89.6, c = 134.9 angstrom and one molecule in the asymmetric unit.
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