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. 2004 May;60(Pt 5):888-94.
doi: 10.1107/S0907444904005232. Epub 2004 Apr 21.

A new highly integrated sample environment for protein crystallography

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A new highly integrated sample environment for protein crystallography

Lilian Jacquamet et al. Acta Crystallogr D Biol Crystallogr. 2004 May.

Abstract

Protein crystallography is becoming a popular technique that is routinely used to access structural information. At one end of the process, sample preparation is now facilitated by commercially available crystallization kits. At the other end, structure determination has been made easier by automated software. Data collection, the step in between, is now usually performed on synchrotron sources. However, it is still restricted to experienced users and requires significant help from beamline staff. Part of this difficulty arises from the sophisticated experimental setup, which comprises a goniometer, a magnetic head, a device for changing the sample and monitoring accessories. It was proposed that this setup could be simplified by replacing these elements by a robotic arm that can perform all of the required tasks. In the present paper, it is demonstrated that this new setup can be used on a synchrotron beamline to mount and centre the sample and to collect diffraction data. This new system completely changes the design of the experimental setup by merging functions that were previously considered to be distinct. Moreover, automation of sample handling need not be considered as a specific development and is now included in a unique multipurpose device.

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