Literature DB >> 22270456

Canadian macromolecular crystallography facility: a suite of fully automated beamlines.

Pawel Grochulski1, Michel Fodje, Shaunivan Labiuk, James Gorin, Kathryn Janzen, Russ Berg.   

Abstract

The Canadian light source is a 2.9 GeV national synchrotron radiation facility located on the University of Saskatchewan campus in Saskatoon. The small-gap in-vacuum undulator illuminated beamline, 08ID-1, together with the bending magnet beamline, 08B1-1, constitute the Canadian Macromolecular Crystallography Facility (CMCF). The CMCF provides service to more than 50 Principal Investigators in Canada and the United States. Up to 25% of the beam time is devoted to commercial users and the general user program is guaranteed up to 55% of the useful beam time through a peer-review process. CMCF staff provides "Mail-In" crystallography service to users with the highest scored proposals. Both beamlines are equipped with very robust end-stations including on-axis visualization systems, Rayonix 300 CCD series detectors and Stanford-type robotic sample auto-mounters. MxDC, an in-house developed beamline control system, is integrated with a data processing module, AutoProcess, allowing full automation of data collection and data processing with minimal human intervention. Sample management and remote monitoring of experiments is enabled through interaction with a Laboratory Information Management System developed at the facility.

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Year:  2012        PMID: 22270456     DOI: 10.1007/s10969-012-9123-9

Source DB:  PubMed          Journal:  J Struct Funct Genomics        ISSN: 1345-711X


  13 in total

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3.  Anomalous signal indicators in protein crystallography.

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Journal:  J Synchrotron Radiat       Date:  2009-01-10       Impact factor: 2.616

5.  Beamline 08ID-1, the prime beamline of the Canadian Macromolecular Crystallography Facility.

Authors:  Pawel Grochulski; Michel N Fodje; James Gorin; Shaunivan L Labiuk; Russ Berg
Journal:  J Synchrotron Radiat       Date:  2011-06-11       Impact factor: 2.616

6.  Processing of X-ray diffraction data collected in oscillation mode.

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  8 in total

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5.  The Stanford Automated Mounter: pushing the limits of sample exchange at the SSRL macromolecular crystallography beamlines.

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6.  The XChemExplorer graphical workflow tool for routine or large-scale protein-ligand structure determination.

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7.  Structure of a VHH isolated from a naïve phage display library.

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8.  A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein.

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  8 in total

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