title: Incorporation of microcrystals by growing protein and virus crystals.
abstract: In the course of time-lapse video and atomic force microscopy (AFM) investigations of macromolecular crystal growth, we frequently observed the sedimentation of microcrystals and three-dimensional nuclei onto the surfaces of much larger, growing protein or virus crystals. This was followed by the direct incorporation over time of the smaller crystals into the bulk of the larger crystals. In some cases, clear indications were present that upon absorption of the small crystal onto the surface of the larger, there was proper alignment of the respective lattices, and consolidation proceeded without observable defect formation, i.e., the two lattices knitted together without discontinuity. In the case of at least one virus crystal, cubic satellite tobacco mosaic virus (STMV), addition of three-dimensional nuclei and subsequent expansion provided the principal growth mechanism at high supersaturation. This process has not been reported for growth from solution of conventional crystals. In numerous other instances, the lattices of the small and larger crystals were obviously misaligned, and incorporation occurred with the formation of some defect. This phenomenon of small crystals physically embedded in larger crystals could only degrade the overall diffraction and materials properties of macromolecular crystals.
authors.affiliation: Department of Biochemistry, University of California Riverside, 92521, USA.
authors.forename: A J
authors.initials: AJ
authors.lastname: Malkin
authors.forename: Y G
authors.initials: YG
authors.lastname: Kuznetsov
authors.forename: A
authors.initials: A
authors.lastname: McPherson
mesh_terms: D003460:Crystallization; D018625:Microscopy, Atomic Force; D010940:Plant Proteins / Q000737:chemistry*; D012526:Satellite Viruses / Q000737:chemistry*; D014027:Tobacco Mosaic Virus / Q000737:chemistry*
chemical_list: D010940:Plant Proteins; C006882:canavalin protein, Canavalia ensiformis