System of primary collimators of SR beam at the small-angle station for KSRS

Ariskin, N.I.; Gerasimov, V. S.; Korneev, V. N.; Sergienko, P.M.; Shishkov, V.I.; Sheromov, M.A.; Stankevich, V. G.; Vazina, A.A.

doi:10.1016/s0168-9002(01)01014-2

Cited by 11 publications

(6 citation statements)

References 3 publications

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“…In addition, the X-ray diffraction experiments were performed at the DICSI small-angle station [8] of the "Siberia-2" storage ring (Russian Research Centre "Kurchatov Institute," Moscow, Russia) with an X-ray film as a detector at a wavelength λ = 0.162 nm (sample-detector distance, 510 nm; exposure time, 10-20 min; I = 70-100 mA).…”

Section: X-ray Diffraction Methodsmentioning

confidence: 99%

“…The capability of synchrotron radiation has given impetus to our long-term investigations of the giant proteoglycan molecules of the extracellular matrix and mucus [2][3][4][5][6][7]. X-ray diffraction and X-ray fluorescence studies of different types of native and modified tissues of man and animals have been performed using several synchrotron sources [2,3,8,9]. This paper reports on the results of comparative Xray diffraction investigations into the structure of proteoglycans of the mucus of the gastrointestinal tract and the extracellular matrix of epithelial tissues in the native state and after different physicochemical actions.…”

Section: Introductionmentioning

confidence: 99%

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Nanostructure ordering of proteoglycans of some biological objects

et al. 2007

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This paper reports on the results of systematic X-ray diffraction investigations into the structure of proteoglycans of the mucus and the extracellular matrix of biological tissues. The small-angle X-ray diffraction patterns of different native and modified tissues of man and animals are measured using synchrotron radiation. A comparative study of the structure of mucins from the mammal and invertebrate mucus is performed. It is demonstrated that the X-ray diffraction patterns of the mammal and invertebrate mucus are very similar to each other and exhibit a number of sharp diffraction rings with a spacing of 4.5 nm and its higher orders due to the highly ordered structure of giant proteoglycan molecules. It is revealed that the proteoglycan structure undergoes a transformation upon interaction with calcium cations. The type of X-ray diffraction pattern ("with a 4.5-nm ring" and "without a ring") for intact tissues can be reversibly changed by treating the tissues in solutions of salts or chelating agents. The inference is made that the X-ray diffraction patterns of tissues can be used as markers for the structural transformation of the extracellular matrix under different exogenous actions.

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Section: X-ray Diffraction Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Nanostructure ordering of proteoglycans of some biological objects

et al. 2007

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“…Photograph 1a shows a part of the station from beamline 1 , which includes the system of primary collimators of synchrotron radiation beam 2 with the focusing crystal monochromator [14,15], the polysectional system of modular blocks of total-externalreflection mirrors 3 [5,16], and evacuated tube 4 for X-ray transmission. Photograph 1b displays the evacuated tube near the measuring system, which involves OD-3-1500 detector 5 and system for the location and life support of samples 6 (for the study of skeletal muscles) [6].…”

Section: Design Features Of the Stationmentioning

confidence: 99%

Development of X-ray equipment for small-angle investigations of biological nanostructures on synchrotron radiation

et al. 2008

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The problems of controlled modernization of equipment for the DICSI small-angle station implemented at the Kurchatov Center for Synchrotron Radiation and Nanotechnology (Russia) are considered. The results of test experiments of software and design improvements for different modes of collection of data on objects are presented. Preliminary tests are performed at the beamline of the VEPP-3 storage ring at the Siberian Synchrotron Center. The "diffraction movie" technique with a high time resolution is developed for investigation of biological structures in static and dynamics states. The results of test experiments with biological objects are analyzed, the designed schemes are justified, and the main parameters of developed X-ray optical systems are discussed.

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“…In addition, the mirrors provide the suppression of higher harmonics of the fundamental wavelength. The four-shutter slits with independent control of each vertical and horizontal shutter are used in order to decrease the level of the background induced by the focusing elements [13,20,21].…”

Section: Equipment and Software Of The Stationmentioning

confidence: 99%

“…The polysectional system of fused-silica mirrors at the 1.3a beamline consists of four independently focusing mirrors (200 × 30 × 6 mm) [20,22]. The mirrors are mounted so that the beam is reflected downward.…”

Section: Equipment and Software Of The Stationmentioning

confidence: 99%

New time-resolved small-angle station with the use of synchrotron radiation of the Siberia-2 storage ring for investigation of biological structures

et al. 2007

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The DICSI small-angle station is developed at the 1.3a beamline of the Siberia-2 storage ring at the Kurchatov Center of Synchrotron Radiation (Russia). The station is intended for X-ray diffraction investigations of the structural dynamics of biological objects with a high time resolution in the small-angle range. The DICSI station is a new version of the station which is based on our previous experience in the development of different stations at the Siberian Synchrotron Center. The OD-3 coordinate detector is used to record the diffraction patterns. The synchrotron beam is monochromatized and collimated with the use of X-ray optical elements, including the system of primary collimators with a focusing monochromator, the polysectional system of focusing mirrors of total external reflection, forming and background slits, a beam attenuator, a primarybeam stop, and evacuated tubes for beam transmission. The station provides measurement of spacings from 1.0 to 100.0 nm in the wavelength range 0.10-0.25 nm with a spectral width ∆λ / λ = 10 -3 -10 -4 .

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System of primary collimators of SR beam at the small-angle station for KSRS

Cited by 11 publications

References 3 publications

Nanostructure ordering of proteoglycans of some biological objects

Nanostructure ordering of proteoglycans of some biological objects

Development of X-ray equipment for small-angle investigations of biological nanostructures on synchrotron radiation

New time-resolved small-angle station with the use of synchrotron radiation of the Siberia-2 storage ring for investigation of biological structures

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