The Small-Angle X-ray Scattering Beamline of the Brazilian Synchrotron Light Laboratory

Kellermann, G.; Vicentin, Flávio C.; Tamura, E.; Rocha, M.; Tolentino, H.; Barbosa, A. F.; Craievich, A. F.; Torriani, Íris L.

doi:10.1107/s0021889897001829

Cited by 141 publications

(102 citation statements)

References 3 publications

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“…Small Angle X-ray Scattering-SAXS experiments were performed at the D11A-SAXS beamline of the Brazilian Sinchrotron Light Laboratory (16). The experimental setup included a temperature-controlled glass capillary (17) and Gabriel type linear position-sensitive detector (18).…”

Section: Methodsmentioning

confidence: 99%

The Pyrococcus Exosome Complex

Ramos

Oliveira

Torriani

et al. 2006

Journal of Biological Chemistry

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The exosome is a conserved eukaryotic enzymatic complex that plays an essential role in many pathways of RNA processing and degradation. Here, we describe the structural characterization of the predicted archaeal exosome in solution using small angle x-ray scattering. The structure model calculated from the small angle x-ray scattering pattern provides an indication of the existence of a disk-shaped structure, corresponding to the "RNases PH ring" complex formed by the proteins aRrp41 and aRrp42. The RNases PH ring complex corresponds to the core of the exosome, binds RNA, and has phosphorolytic and polymerization activities. Three additional molecules of the RNA-binding protein aRrp4 are attached to the core as extended and flexible arms that may direct the substrates to the active sites of the exosome. In the presence of aRrp4, the activity of the core complex is enhanced, suggesting a regulatory role for this protein. The results shown here also indicate the participation of the exosome in RNA metabolism in Archaea, as was established in Eukarya.

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Section: Methodsmentioning

confidence: 99%

The Pyrococcus Exosome Complex

Ramos

Oliveira

Torriani

et al. 2006

Journal of Biological Chemistry

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“…SAXS-Small angle x-ray scattering experiments were performed at the SAS beam line of the LNLS synchrotron radiation facility, Campinas, Brazil (31). Measurements were make with a monochromatic x-ray beam with a wavelength ϭ 1.488 Å for a sample-detector distance of 840 mm covering the momentum transfer range 0.01 Ͻ q Ͻ 0.44 Å -1 (q ϭ 4 sin / , where 2 is the scattering angle).…”

Section: Methodsmentioning

confidence: 99%

Free Human Mitochondrial GrpE Is a Symmetric Dimer in Solution

Borges

Fischer

Craievich

et al. 2003

Journal of Biological Chemistry

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The co-chaperone GrpE is essential for the activities of the Hsp70 system, which assists protein folding. GrpE is present in several organisms, and characterization of homologous GrpEs is important for developing structure-function relationships. Cloning, producing, and conformational studies of the recombinant human mitochondrial GrpE are reported here. Circular dichroism measurements demonstrate that the purified protein is folded. Thermal unfolding of human GrpE measured both by circular dichroism and differential scanning calorimetry differs from that of prokaryotic GrpE. Analytical ultracentrifugation data indicate that human GrpE is a dimer, and the sedimentation coefficient agrees with an elongated shape model. Small angle x-ray scattering analysis shows that the protein possesses an elongated shape in solution and demonstrates that its envelope, determined by an ab initio method, is similar to the high resolution envelope of Escherichia coli GrpE bound to DnaK obtained from single crystal x-ray diffraction. However, in these conditions, the E. coli GrpE dimer is asymmetric because the monomer that binds DnaK adopts an open conformation. It is of considerable importance for structural GrpE research to answer the question of whether the GrpE dimer is only asymmetric while bound to DnaK or also as a free dimer in solution. The low resolution structure of human GrpE presented here suggests that GrpE is a symmetric dimer when not bound to DnaK. This information is important for understanding the conformational changes GrpE undergoes on binding to DnaK.

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“…The samples were centrifuged for 15 min at 13.000xg (at 10ºC) prior to the SAXS measurements and the GndHCl addition. All data were collected on the SAXS synchrotron beamline at the LNLS (Campinas, Brazil) [39]. The wavelength of the incident monochromatic X-ray beam was λ = 1.488 Å.…”

Section: Small-angle X-ray Scattering (Saxs)mentioning

confidence: 99%

Probing conformational changes in orphan nuclear receptor: The NGFI-B intermediate is a partially unfolded dimer

Garcia¹,

Figueira²,

Neto³

et al. 2008

Biophysical Chemistry

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT

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The Small-Angle X-ray Scattering Beamline of the Brazilian Synchrotron Light Laboratory

Cited by 141 publications

References 3 publications

The Pyrococcus Exosome Complex

The Pyrococcus Exosome Complex

Free Human Mitochondrial GrpE Is a Symmetric Dimer in Solution

Probing conformational changes in orphan nuclear receptor: The NGFI-B intermediate is a partially unfolded dimer

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