Quantitive evaluation of macromolecular crystallization experiments using 1,8-ANS fluorescence

Modern X‐ray structure analysis and advances in high‐throughput robotics have allowed a significant increase in the number of conditions screened for a given sample volume. An efficient evaluation of the increased amount of crystallization trials in order to identify successful experiments is now ur...

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Bibliographic Details

Published in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2010-08, Vol.66 (8), p.901-908
Main Authors:	Watts, David, Müller-Dieckmann, Jochen, Tsakanova, Gohar, Lamzin, Victor S., Groves, Matthew R.
Format:	Article
Language:	English
Subjects:	Anilino Naphthalenesulfonates - analysis Animals Crystallization Crystallography, X-Ray - methods Endopeptidase K - chemistry fluorescence high-throughput crystallization image analysis Muramidase - chemistry Plasmodium falciparum - enzymology protein crystallization Software
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