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Title: Biological, Macromolecular Switches and Cyclers

; ; ;  [1];  [2]
  1. UW
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
Resource Type:
Journal Article
Resource Relation:
Journal Name: Rom. J. Biochem.; Journal Volume: 47; Journal Issue: 2
Country of Publication:
United States

Citation Formats

Ulijasz, Andrew T., Purwar, Namrta, Srajer, Vukica, Schmidt, Marius, and UC). Biological, Macromolecular Switches and Cyclers. United States: N. p., 2014. Web.
Ulijasz, Andrew T., Purwar, Namrta, Srajer, Vukica, Schmidt, Marius, & UC). Biological, Macromolecular Switches and Cyclers. United States.
Ulijasz, Andrew T., Purwar, Namrta, Srajer, Vukica, Schmidt, Marius, and UC). Thu . "Biological, Macromolecular Switches and Cyclers". United States. doi:.
title = {Biological, Macromolecular Switches and Cyclers},
author = {Ulijasz, Andrew T. and Purwar, Namrta and Srajer, Vukica and Schmidt, Marius and UC)},
abstractNote = {},
doi = {},
journal = {Rom. J. Biochem.},
number = 2,
volume = 47,
place = {United States},
year = {Thu Aug 14 00:00:00 EDT 2014},
month = {Thu Aug 14 00:00:00 EDT 2014}
  • Resolution in transmission electron microscopy (TEM) now is limited by the properties of specimens, rather than by those of instrumentation. The long-standing difficulties in obtaining truly high-resolution structure from biological macromolecules with TEM demand the development, testing, and application of new ideas and unconventional approaches. This review concisely describes some new concepts and innovative methodologies for TEM that deal with unsolved problems in the preparation and preservation of macromolecular specimens. The selected topics include use of better support films, a more protective multi-component matrix surrounding specimens for cryo-TEM and negative staining, and, several quite different changes in microscopy and micrographymore » that should decrease the effects of electron radiation damage; all these practical approaches are non-traditional, but have promise to advance resolution for specimens of biological macromolecules beyond its present level of 3-10 {angstrom} (0.3-1.0 nm). The result of achieving truly high resolution will be a fulfillment of the still unrealized potential of transmission electron microscopy for directly revealing the structure of biological macromolecules down to the atomic level.« less
  • No abstract prepared.
  • To reveal the function of the biological macromolecular assemblies at atomic level, three-dimensional structure of the complex molecules is essential. The beamline including detectors is designed to collect high resolution and high quality diffraction data from macromolecular assembly crystals with large unit cells. This beamline uses a standard undulator of SPring-8 as a light source. X-rays from the undulator are monochromatized by a liquid nitrogen cooled double crystal. The monochromatized X-ray beam is collimated or focused reflected by a Rhodium-coated mirror, and it is also used for elimination of higher-order harmonics. At downstream of the Beryllium window, we place amore » fast shutter system, two quadrant slit systems, and an ionization chamber in this order. Size of the X-ray-beam can be changed by the slit systems from 1 {mu}m to fully-open. Typical photon flux is about 1011 photons/sec. with the slit size of 0.07 x 0.07 mm2 at 0.9 A. A sample is cooled either to 90K by a nitrogen or to 30K by a helium cryo-stream system. A DIP6040, which is a hybrid-type of image plates and a CCD, is used for data collection. The DIP6040 has six image plates with individual readout systems, and effective area of each image plate is circular with 400 mm in diameter. A 185 mm{phi} CCD detector can be used both for data collection and screening of the crystals. Frame rate of the image plate system can be achieved to 120 images per hour at maximum.« less
  • Beamline BL44XU at SPring-8 is operated by the Institute for Protein Research of Osaka University. The beamline is designed for X-ray crystallography of large biological macromolecular assemblies. Here we show its detailed performances, results, and the ongoing upgrade plans.