AVS 50th International Symposium
    Biomaterial Interfaces Monday Sessions
       Session BI-MoM

Paper BI-MoM10
In situ Real-time Atomic Force Microscopy Studies of Lysozyme and RR02 Protein Crystal Growth at Surfaces

Monday, November 3, 2003, 11:20 am, Room 307

Session: Protein-Surface Interactions
Presenter: S.J.B. Tendler, University of Nottingham, UK
Authors: T.R. Keel, University of Nottingham, UK
S. Allen, University of Nottingham, UK
M.C. Davies, University of Nottingham, UK
C.J. Roberts, University of Nottingham, UK
S.J.B. Tendler, University of Nottingham, UK
P.M. Williams, University of Nottingham, UK
Correspondent: Click to Email
The successful application of crystallography to fields such as structural biology and rational drug design has been largely due to the availability of single crystals of the macromolecule of interest. However, relatively little is understood about the fundamentals of macromolecular crystal growth. Here, we have utilized the technique of atomic force microscopy (AFM) to study protein growth at surfaces. Two different protein systems, at both the micro- and nanometre scale have been investigated. The first is a model system, lysozyme. We have investigated two polymorphs of the lysozyme crystal and present data concerning the effect of supersaturation (@sigma@) on the growth rates and mechanisms of growth of the crystals. Molecular resolution studies have also been carried out and the observed periodicities are in good agreement with the known unit cell dimensions. Also presented are preliminary results from a second protein system, RR02, which is a response regulator protein found in streptococcus pneumoniae. RR02 is relatively straightforward to crystallize, but unlike lysozyme, many of the grown crystals diffract poorly and x-ray studies yield little structural data. We have used the AFM to investigate these crystals and compare the results with the lysozyme studies.