The crystallography beamline I711 at MAX II

Cerenius, Yngve; Ståhl, Kenny; Svensson, L.A.; Ursby, Thomas; Oskarsson, Åke; Albertsson, J.; Liljas, Anders

doi:10.1107/s0909049500005331

Cited by 219 publications

(178 citation statements)

References 8 publications

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“…Synchrotron SAXS data for CaM and the CaM-cx43-CBD complex were collected on beamline I711 at MAX-Lab, Lund, Sweden [20]. Data processing was done using the in-house Bli711 software, and programs from the ATSAS package [21] were used for data analysis and molecular modeling.…”

Section: Small-angle X-ray Scatteringmentioning

confidence: 99%

Complex formation between calmodulin and a peptide from the intracellular loop of the gap junction protein connexin43: Molecular conformation and energetics of binding

Myllykoski

Kuczera

Kursula

2009

Biophysical Chemistry

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. Complex formation between calmodulin and a peptide from the intracellular loop of the gap junction protein connexin43: Molecular conformation and energetics of binding. Biophysical Chemistry, Elsevier, 2009, 144 (3) 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 AbstractGap junctions are formed by a family of transmembrane proteins, connexins.Connexin43 is a widely studied member of the family, being ubiquitously expressed in a variety of tissues and a target of a large number of disease mutations. The intracellular loop of connexin43 has been shown to include a calmodulin binding domain, but detailed 3-dimensional data on the structure of the complex are not available. In this study, we used a synthetic peptide from this domain to reveal the conformation of the calmodulin-peptide complex by small angle X-ray scattering.Upon peptide binding, calmodulin lost its dumbbell shape, adopting a more globular conformation. We also studied the energetics of the interaction using calorimetry and computational methods. All our data indicate that calmodulin binds to the peptide from cx43 in the classical 'collapsed' conformation.

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Section: Small-angle X-ray Scatteringmentioning

confidence: 99%

Complex formation between calmodulin and a peptide from the intracellular loop of the gap junction protein connexin43: Molecular conformation and energetics of binding

Myllykoski

Kuczera

Kursula

2009

Biophysical Chemistry

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“…The sample was loaded into a hole (0.15 mm diameter, 0.1 mm depth) in the stainlesssteel gasket placed in-between the diamonds. The data were collected at MAX-Lab (Lund, Sweden) I711 beamline [22] with wavelength of 0.91985 Å, using a MAR165 detector. The FIT2D program [23] was used for conversion of the 2D data to 1D.…”

Section: Methodsmentioning

confidence: 99%

Equation of state of CaMnO3: a combined experimental and computational study

et al. 2013

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“…SR-PXD data for sample S2-200 were measured at the MAX-II synchrotron at beamline I711 in the research laboratory MAXlab, Lund, Sweden using a MAR165 CCD detector system. 34 The sample was mounted in sapphire (Al 2 O 3 ) single crystal tubes (0.79 mm i.d.) in an argon-filled glovebox.…”

Section: Theoretical Calculationsmentioning

confidence: 99%

Hydrogen–fluorine exchange in NaBH4–NaBF4

Rude

Filsø

D’Anna

et al. 2013

Phys. Chem. Chem. Phys.

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a Hydrogen-fluorine exchange in the NaBH 4 -NaBF 4 system is investigated using a range of experimental methods combined with DFT calculations and a possible mechanism for the reactions is proposed. Fluorine substitution is observed using in situ synchrotron radiation powder X-ray diffraction (SR-PXD) as a new Rock salt type compound with idealized composition NaBF 2 H 2 in the temperature range T = 200 to 215 1C. Combined use of solid-state 19 F MAS NMR, FT-IR and DFT calculations supports the formation of a BF 2 H 2 complex ion, reproducing the observation of a 19 F chemical shift at 144.2 ppm, which is different from that of NaBF 4 at 159.2 ppm, along with the new absorption bands observed in the IR spectra. After further heating, the fluorine substituted compound becomes X-ray amorphous and decomposes to NaF at B310 1C. This work shows that fluorine-substituted borohydrides tend to decompose to more stable compounds, e.g. NaF and BF 3 or amorphous products such as closo-boranes, e.g. Na 2 B 12 H 12 . The NaBH 4 -NaBF 4 composite decomposes at lower temperatures (300 1C) compared to NaBH 4 (476 1C), as observed by thermogravimetric analysis. NaBH 4 -NaBF 4 (1 : 0.5) preserves 30% of the hydrogen storage capacity after three hydrogen release and uptake cycles compared to 8% for NaBH 4 as measured using Sievert's method under identical conditions, but more than 50% using prolonged hydrogen absorption time. The reversible hydrogen storage capacity tends to decrease possibly due to the formation of NaF and Na 2 B 12 H 12 . On the other hand, the additive sodium fluoride appears to facilitate hydrogen uptake, prevent foaming, phase segregation and loss of material from the sample container for samples of NaBH 4 -NaF.

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The crystallography beamline I711 at MAX II

Cited by 219 publications

References 8 publications

Complex formation between calmodulin and a peptide from the intracellular loop of the gap junction protein connexin43: Molecular conformation and energetics of binding

Complex formation between calmodulin and a peptide from the intracellular loop of the gap junction protein connexin43: Molecular conformation and energetics of binding

Equation of state of CaMnO3: a combined experimental and computational study

Hydrogen–fluorine exchange in NaBH4–NaBF4

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