title: Optimization of the critical nuclear size for protein crystallization: a note.
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.
authors.affiliation: The Biochemistry Laboratory, Biology Department, University of Athens, Panepistimiopolis, Athens 15 701, Greece. e.saridakis@ic.ac.uk
authors.forename: E
authors.initials: E
authors.lastname: Saridakis
mesh_terms: D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D008956:Models, Chemical; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D012996:Solutions
chemical_list: D011506:Proteins; D012996:Solutions