Tuesday, August 23, 2022
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Saturday, August 27, 2022
Palais des Congrès de Versailles
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Crystallization and biophysical characterization
27 August 2022
1
,
Live
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MS3
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14:00
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16:00
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Crystallization and biophysical characterization
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Richelieu Amphithéâtre
14:00
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INT21
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Successful sample preparation for serial crystallography at synchrotrons and XFELs
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J.
John
BEALE
Content :
The applications and potential advantages of serial crystallography, at both synchrotron and XFEL light sources, are growing. Despite advances in delivery methods, the sample volumes of micro-crystals required for serial crystallography, particularly time-resolved experiments, are still demanding. Batch crystallisation methods are the primary means in crystallographers toolbox to create these samples. However, the process to convert single crystals grown by vapour diffusion to large volumes (> 100 µL) of micro-crystalline slurry can be exceptionally challenging.
To try and ease the process, we have formulated a strategy to perform this translation. It is divided into three stages: (1) optimising crystal morphology, (2) transitioning to batch, and (3) scaling. Given the variation of protein crystallisation, we hope that this protocol can act as a useful framework when attempting the conversion from vapour diffusion to batch.
In this talk, I will explain how this process was developed and applied to model proteins. Then I will talk about some of the experiences, good and bad, we have had with user proteins at the SLS and SwissFEL. I will finish with a peak at some results from how this user crystals fared at the new SwissFEL endstation, Cristallina.
14:30
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769
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Protein quality control for improved data reproducibility and reliability
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K.
Kim
REMANS
15:00
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524
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Serial crystallography: a game-changer in crystallization and crystal handling
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C.
Claude
SAUTER
15:20
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495
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Screening approaches that explore chemical space in order to identify suitable starting conditions for structure determination by cryoEM or other methods
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P.
Patrick D.
SHAW STEWART
15:40
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312
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Nucleation and reproducibility in protein crystallization assisted by the crystallophore.
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E.
Eric
GIRARD
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