<i>DENZO</i> and <i>SCALEPACK</i>

Otwinowski, Zbyszek; Minor, Władek; Borek, Dominika; Cymborowski, M.

doi:10.1107/97809553602060000677

Cited by 186 publications

(195 citation statements)

References 37 publications

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“…The temperature was controlled using an Oxford Cryosystem low temperature device, operating at 120 K. Data collection was carried out using the COL-LECT program [24]. Integration and scaling of the reflections were performed with the HKL Denzo-Scalepack system of programs [25] and numerical absorption corrections were performed [26]. The structure was solved using direct methods with SHELXS-97 [27].…”

Section: X-ray Data Collection and Structure Determinationmentioning

confidence: 99%

Pt(II) and Ag(I) complexes with acesulfame: Crystal structure and a study of their antitumoral, antimicrobial and antiviral activities

Cavicchioli

Massabni

Heinrich

et al. 2010

Journal of Inorganic Biochemistry

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Section: X-ray Data Collection and Structure Determinationmentioning

confidence: 99%

Pt(II) and Ag(I) complexes with acesulfame: Crystal structure and a study of their antitumoral, antimicrobial and antiviral activities

Cavicchioli

Massabni

Heinrich

et al. 2010

Journal of Inorganic Biochemistry

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“…Diffraction data were collected using graphite-monochromated Mo-K α radiation with an Enraf-Nonius KappaCCD diffractometer at 150(1) K [Cryostream Cooler (Oxford Cryosystem)] and analyzed using the HKL DENZO program package (ref. [33] ). Cell parameters were determined from all data by the same program package.…”

Section: X-ray Measurementmentioning

confidence: 99%

“…Cell parameters were determined from all data by the same program package. [33] The structure was solved by direct methods (SIR 97 [34] ) and refined by full-matrix least-squares techniques (SHELXL97 [35] ). The used scattering factors for neutral atoms were included in the SHELXL97 program.…”

Section: X-ray Measurementmentioning

confidence: 99%

Study of Thermodynamic and Kinetic Stability of Transition Metal and Lanthanide Complexes of DTPA Analogues with a Phosphorus Acid Pendant Arm

et al. 2006

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The thermodynamic and kinetic stabilities of the complexes of phosphonate and phenylphosphinate analogues of H 5 dtpa with selected transition-and lanthanide-metal ions are presented. Both phosphorus-containing ligands form thermodynamically very stable complexes, with stability constants comparable with or even higher than those reported for the parent H 5 dtpa. However, the kinetic inertness of their gadolinium(III) complexes against acid-and metal-assisted decomplexations is surprisingly much lower. The half-life times of gadolinium(III) complexes of the new ligands in the pres-

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“…For model building and refinement, a two-pass high-resolution data set was collected from another crystal at a wavelength of 0.9641 Å. The data were analyzed and reduced to averaged intensities by using HKL2000 (34,35). Intensities were converted to structure factor amplitudes by using programs from the CCP4 suite (36,37).…”

Section: Resultsmentioning

confidence: 99%

Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation

Colbert¹,

Erbel

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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The covalent attachment of heme cofactors to the apo-polypeptides via thioether bonds is unique to the maturation of c-type cytochromes. A number of thiol-disulfide oxidoreductases prepare the apocytochrome for heme insertion in system I and II cytochrome c maturation. Although most thiol-disulfide oxidoreductases are nonspecific, the less common, specific thiol-disulfide oxidoreductases may be key to directing the usage of electrons. Here we demonstrate that unlike other thiol-disulfide oxidoreductases, the protein responsible for reducing oxidized apocytochrome c in Bacillus subtilis, ResA, is specific for cytochrome c550 and utilizes alternate conformations to recognize redox partners. We report solution NMR evidence that ResA undergoes a redox-dependent conformational change between oxidation states, as well as data showing that ResA utilizes a surface cavity present only in the reduced state to recognize a peptide derived from cytochrome c550. Finally, we confirm that ResA is a specific thiol-disulfide oxidoreductase by comparing its reactivity to our mimetic peptide with its reactivity to oxidized glutathione, a nonspecific substrate. This study biochemically demonstrates the specificity of this thioldisulfide oxidoreductase and enables us to outline a structural mechanism of regulating the usage of electrons in a thiol-disulfide oxidoreductase system. NMR ͉ thiol-disulfide oxidoreductase ͉ x-ray crystallography

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DENZO and SCALEPACK

Cited by 186 publications

References 37 publications

Pt(II) and Ag(I) complexes with acesulfame: Crystal structure and a study of their antitumoral, antimicrobial and antiviral activities

Pt(II) and Ag(I) complexes with acesulfame: Crystal structure and a study of their antitumoral, antimicrobial and antiviral activities

Study of Thermodynamic and Kinetic Stability of Transition Metal and Lanthanide Complexes of DTPA Analogues with a Phosphorus Acid Pendant Arm

Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation

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