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Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
Published on: November 1, 2012
Optimization of the critical nuclear size for protein crystallization: a note
1The Biochemistry Laboratory, Biology Department, University of Athens, Panepistimiopolis, Athens 15 701, Greece. e.saridakis@ic.ac.uk
Acta Crystallographica. Section D, Biological Crystallography
|February 10, 2000
Abstract:
It was observed that for some proteins the best crystals for X-ray diffraction have been obtained at supersaturation ratios of ca 2.5-3 (in experiments without seeding). It was then noticed that under certain conditions specific to the protein such values are close to a local minimum of the critical radius for nucleation. A relation between the two observations is proposed.
