title: Enhancing drop stability in protein crystallization by chemical patterning.
abstract: The motion of protein drops on crystallization media during routine handling is a major factor affecting the reproducibility of crystallization conditions. Drop stability can be enhanced by chemical patterning to more effectively pin the drop's contact line. As an example, a hydrophilic area is patterned on an initially flat hydrophobic glass slide. The drop remains confined to the hydrophilic area and the maximum drop size that remains stable when the slide is rotated to the vertical position increases. This simple method is readily scalable and has the potential to significantly improve the outcomes of hanging-drop and sitting-drop crystallization.
authors.affiliation: Cornell University, Ithaca, NY 14853, USA. vb54@cornell.edu
authors.forename: Viatcheslav
authors.initials: V
authors.lastname: Berejnov
authors.forename: Robert E
authors.initials: RE
authors.lastname: Thorne
mesh_terms: D003460:Crystallization / Q000379:methods*; D018625:Microscopy, Atomic Force; D008956:Models, Chemical; D009113:Muramidase / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties; D013500:Surface Tension
chemical_list: D011506:Proteins; D009113:Muramidase