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The National Institutes of Health (NIH), through its National Institute of General Medical Sciences (NIGMS), funds MacCHESS for two purposes: core research as motivated by the important biomedical problems and support to all structural biologists making use of the CHESS facility for crystallographic and small-angle X-ray scattering experiments, as well as for novel experiments requiring special equipment and staff assistance not readily available at other synchrotron sources. Macromolecular Diffraction at the Cornell High Energy Synchrotron Source (MacCHESS) provides a facility for developing new technology and for advancing the research goals of structural biologists as well as the broader biological research community. MacCHESS has a strong commitment to training future leaders, who will be able to translate advances in synchrotron science and structural biology into valuable biomedical applications. Guidance in determining MacCHESS's major emphases is provided by the MacCHESS Advisory Committee.

Structural insight into HIV reverse transcriptase

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Arnold and DeStefano then collaborated to study the aptamer using structural biology. Not only did they manage to solve the structure of the RT-aptamer complex, they found that the new inhibitor bound so tightly to RT that it stabilizes the complex and helps it to form better crystals than were previously available.

Humanity helper: CHESS-made device rode into space

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The In-Situ-1 crystallization plate, developed by Mi-Te-Gen and its founder, Robert Thorne, is shown along with a patch from the SpaceX CRS-8 mission in April, on which the plate flew for experiments by drugmaker Eli Lilly.

Long-range electron transfer in the cytochrome c peroxidase and cytochrome c complex requires stringent conditions

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Mitochondrial cytochrome c peroxidase (CcP) binds to cytochrome c (Cc) to break down hydrogen peroxide to water. This reaction is a series of steps that involves heme-oxygen chemistry and long-range electron transfer (ET)

Workshop #2 recap: Biomolecules in Motion

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This “biomolecules” workshop was held on June 8th. This workshop focuses on motion of biomolecules (proteins, nucleic acids, complexes) which occurs as they perform their functions. “Motion” includes conformational changes, ranging from large domain “hinging” motions to relatively small loop motions (e.g. to allow and deny access to an active site); oligomerization changes; interaction with partner molecules.


CHESS Scheduled X-ray Runs:
2016: October 26 - December 13
2017: January 25 - March 7
2017: March 15 - April 24
2017: May 17 - June 29
2017: October 11 - December 21

Proposal Submission

MacCHESS User Info

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MacCHESS provides a facility for developing new technology and for advancing the research goals of structural biologists as well as the broader biological research community.

Microcrystallography

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Microcrystallography refers to the ability to obtain useful structures from small (<30 μm) crystals...

BioSAXS

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Small-Angle X-Ray Solution Scattering (SAXS) at MacCHESS. Protein envelope reconstruction...

BioSAXS Essentials training course

Automation

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Automounters are intended to help maximize throughput at synchrotron beam lines where heavy shielding and safety interlocks slow manual access to the experiment...

High Pressure cooling

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Having constructed and tested the necessary equipment at CHESS, pressure-cryocooling is available to the user community on an experimental basis