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Faculty of Chemistry, Jagiellonian University, Kraków

Dr. Joanna Loch
Faculty of Chemistry, Jagiellonian University

 

Dr. Joanna Loch is Assistant Professor in the Department of Crystal Chemistry and Crystal Physics in Faculty of Chemistry, Jagiellonian University, Kraków. Dr. Loch is a specialist structural biologist / protein crystallographer. Much of Dr. Loch’s recent research has concentrated on various aspects of β-Lactoglobulin: one of the principal whey proteins, and therefore of huge importance to the food industry. Prior to the recent installation of their new Rigaku Oxford Diffraction XtaLAB Synergy-S (Mo, Cu) / HyPix-6000HE diffractometer system, the Crystal Chemistry and Crystal Physics team in Jagiellonian University have depended upon their Oxford Diffraction SuperNova system: installed in 2009. The two instruments are shared between a large number of researchers. As well as structural biology (including crystallographic studies of proteins under high pressure: contained in diamond anvil cells), other major themes of study in the Department include, particularly, high resolution data-collection and charge-density analysis, and supporting the range of synthetic chemistry and materials research in the Faculty of Chemistry.

Dr. Loch explains the benefits in using the XtaLAB Synergy-S system, below.

What was the main problem or challenge you were trying to solve by buying a new diffractometer system?

We wanted to have a possibility to speed-up experiments for protein crystals in order to test diffraction before synchrotron data collection or have the possibility to collect high-quality diffraction data for protein crystals without the use of the synchrotron.

How has the new instrument from Rigaku Oxford Diffraction changed the workflow in your lab?

A new instrument significantly improved the quality of collected data due to the use of a highly focused X-ray beam and great detector enabling very fast data recording. These elements allowed to speed up our work and collect data even for 4-6 protein crystals per day (24 h). When we were using SuperNova, it was possible to collect data only for 1 crystal per day (usually 14-18 h needed for data collection for one crystal).

Can you describe the single most important benefit the XtaLAB Synergy-S system brings to your research?

The most important benefit is time: using XtaLAB Synergy-S can save a lot of time and I can work even 6-times faster!!!

Which other features of the XtaLAB Synergy-S system are important to you ?

It is easier and faster to mount and center crystal prior to data collection (goniometer moves much faster in comparison to SuperNova), I also like the new software.

What would you say to anyone considering making a purchase of a new high-capability diffractometer?

I would recommend the XtaLAB Synergy-S system for structural biology labs because it is very useful for checking the diffraction quality of protein crystals and allow to collect high-quality data for “non-problematic”, well-diffracting protein crystals. In my opinion, the quality of the data is comparable to those collected at some not-highly intensive synchrotron beamlines, as e.g. SBC beamline 19-BM at the APS (Argonne National Laboratory).

Is there anything else that you would like to add about your experience of working with Rigaku Oxford Diffraction?

It is very important to me as a user that I have support from Rigaku Oxford Diffraction when I need to process problematic data. To date, I have several problematic datasets, and every time I had a problem with the processing of the data, I got help from the Rigaku Team, and I was able to solve the structure.