John Chrzas

University of Georgia, Атина, Georgia, United States

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Publications (8)26.51 Total impact

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    ABSTRACT: The crystal structure of the 11.14 kDa orphan ORF 1382 from Archaeoglobus fulgidus (AF1382) has been determined by sulfur SAD phasing using a moderately diffracting crystal and 1.9 Å wavelength synchrotron X-rays. AF1382 was selected as a structural genomics target by the Southeast Collaboratory for Structural Genomics (SECSG) since sequence analyses showed that it did not belong to the Pfam-A database and thus could represent a novel fold. The structure was determined by exploiting longer wavelength X-rays and data redundancy to increase the anomalous signal in the data. AF1382 is a 95-residue protein containing five S atoms associated with four methionine residues and a single cysteine residue that yields a calculated Bijvoet ratio (ΔF(anom)/F) of 1.39% for 1.9 Å wavelength X-rays. Coupled with an average Bijvoet redundancy of 25 (two 360° data sets), this produced an excellent electron-density map that allowed 69 of the 95 residues to be automatically fitted. The S-SAD model was then manually completed and refined (R = 23.2%, R(free) = 26.8%) to 2.3 Å resolution (PDB entry 3o3k). High-resolution data were subsequently collected from a better diffracting crystal using 0.97 Å wavelength synchrotron X-rays and the S-SAD model was refined (R = 17.9%, R(free) = 21.4%) to 1.85 Å resolution (PDB entry 3ov8). AF1382 has a winged-helix-turn-helix structure common to many DNA-binding proteins and most closely resembles the N-terminal domain (residues 1-82) of the Rio2 kinase from A. fulgidus, which has been shown to bind DNA, and a number of MarR-family transcriptional regulators, suggesting a similar DNA-binding function for AF1382. The analysis also points out the advantage gained from carrying out data reduction and structure determination on-site while the crystal is still available for further data collection.
    Acta Crystallographica Section D Biological Crystallography 09/2012; 68(Pt 9):1242-52. DOI:10.1107/S0907444912026212 · 7.23 Impact Factor
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    ABSTRACT: Familial oncocytic thyroid carcinoma is associated with a missense mutation, P308Q, in the C-terminal domain of Tim44. Tim44 is the mitochondrial inner-membrane translocase subunit and it functions as a membrane anchor for the mitochondrial heat-shock protein 70 (mtHsp70). Here, the crystal structure of the human Tim44 C-terminal domain complexed with pentaethylene glycol has been determined at 1.9 A resolution. The overall structure resembles that of the nuclear transport factor 2-like domain. In the crystal structure, pentaethylene glycol molecules are associated at two potential membrane-binding sites: the large hydrophobic cavity and the highly conserved loop between the alpha1 and alpha2 helices near Pro308. A comparison with the yeast homolog revealed that lipid binding induces conformational changes around the alpha1-alpha2 loop, leading to slippage of the alpha1 helix along the large beta-sheet. These changes may play important roles in the translocation of polypeptides across the mitochondrial inner membrane.
    Acta Crystallographica Section D Biological Crystallography 01/2008; 63(Pt 12):1225-34. DOI:10.1107/S0907444907051463 · 7.23 Impact Factor
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    ABSTRACT: A parallel algorithm has been designed for SHELXD to solve the heavy-atom partial structures of protein crystals quickly. Based on this algorithm, a program has been developed to run on high-performance multiple-CPU Linux PCs, workstations or clusters. Tests on the 32-CPU Linux cluster at SER-CAT, APS, Argonne National Laboratory, show that the parallelization dramatically speeds up the process by a factor of roughly the number of CPUs applied, leading to reliable and instant heavy-atom sites solution, which provides the practical opportunity to employ heavy-atom search as an alternative tool for anomalous scattering data quality evaluation during single/multiple-wavelength anomalous diffraction (SAD/MAD) data collection at synchrotron beamlines.
    Journal of Applied Crystallography 04/2007; 40(2):390-390. DOI:10.1107/S0021889807003998 · 3.95 Impact Factor
  • Acta Crystallographica Section A Foundations of Crystallography 08/2005; 61. DOI:10.1107/S0108767305094183 · 2.07 Impact Factor
  • Acta Crystallographica Section A Foundations of Crystallography 08/2002; 58. DOI:10.1107/S0108767302086233 · 2.07 Impact Factor
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    ABSTRACT: MurF is required to catalyze the final step in the synthesis of the cytoplasmic precursor of the bacterial cell wall peptidoglycan, rendering it an attractive target for antibacterial drug development. The crystal structure of the MurF apo-enzyme has been determined using the multiwavelength anomalous dispersion method and refined to 2.3 A resolution. It contains three consecutive open alpha/beta-sheet domains. In comparison with the complex crystal structures of MurD and its substrates, The topology of the N-terminal domain of MurF is unique, while its central and C-terminal domains exhibit similar mononucleotide and dinucleotide-binding folds, respectively. The apo-enzyme of MurF crystal structure reveals an open conformation with the three domains juxtaposed in a crescent-like arrangement creating a wide-open space where substrates are expected to bind. As such, catalysis is not feasible and significant domain closure is expected upon substrate binding.
    Journal of Molecular Biology 01/2001; 304(3):435-45. DOI:10.1006/jmbi.2000.4215 · 3.96 Impact Factor
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    ABSTRACT: A simple and robust design for the liquid nitrogen-cooled first monochromator crystal suitable for large Bragg-angles has been implemented at three undulator beamlines at the Advanced Photon Source (IMCA CAT, BioCAT, and MR CAT). The design features a simple and reliable seal and a strain free mount. The system has been pressure tested intentionally and accidentally to failure and the crystal reseals. Measurements have been made under closed gap conditions with little indication of distortion. The crystal design, implementation and measurements are presented
    AIP Conference Proceedings 01/2000; DOI:10.1063/1.1291799