Dear bionet.xtallography readers:
The following mail message is being sent to Macromolecular SIG members
of the ACA. It relates to the ACA meeting to be held in Saint Louis from
July 20 to 25, 1997. The mailing list was kindly provided by the ACA
membership office. In a previous mailing we found that approximately 25% of
the e-Mail addresses in the current listing are incorrect. Please let us
know if you wish to be included in further mailings on the session, and
please respond to this request for input for the session.
Thanks,
Joe and George
_____________________________________________________________________________
Herewith follows a list of topics suggested by many of you for the SIG
sponsored session on crystal growth. In addition to this list please note
Madeleine Ries-Kautt, C.N.R.S. Gif-sur-Yvette, and Marc Pusey, NASA Marshall
Space Flight Center, have agreed to deliver keynote lectures at the session.
Dr. Ries-Kautt will introduce the macromolecular crystallization problem
and discuss physical-chemical strategies to tackle the problem. Dr. Pusey
will deliver a critical review of crystal growth in a microgravity
enviornment.
With a limited amount of time allotted, we must identify at most
one or two topics upon which we might focus the session. We are asking your
advice on the selection. Please indicate, in order of preference, the
THREE topics you would like to hear about at the session. Indicate by letter,
and then if you can, indicate a speaker who might address the topic. For
example: A (Jane Smith), F (John Smith), M (Jean Smith). If, in addition,
you feel a serious error of omission in the list has been made, feel free to
tell us so. Respond to us at the addresses below.
A. The use of monoclonal antibodies as crystallization tools.
B. Rational use of site-directed mutagenesis to engineer protein-protein
contacts that foster crystallization. This would include methods to
analyze protein-protein contacts in the crystal lattice.
C. The role of microgravity in crystal growth.
D. The special problems of membrane-bound protein crystallizations.
E. Nucleic acid (DNA, RNA) crystallization.
F. A review of physical methods for studying crystallization mechanisms.
G. The problems of multi-domain proteins with flexible hinge regions.
H. The use of crystallization databases as tools for crystal growth.
I. The preparation of crystals of enzyme/inhibitor complexes.
J. The problems of inhomogeneous sample preparations, such as might be
seen in preps with minor contaminants, with heterogeneous glycosylation,
etc. This would include chemical and biochemical methods to assess
homogeneity.
K. Fab crystallization.
L. Atomic force microscopy results.
M. Physical methods other than diffraction that may be useful in assessing
crystal quality. This would include spectrophotometric methods to study
protein-protein interactions in solution.
N. The latest methods to determine solubility diagrams.
O. The latest on crystallizing agents.
P. Quantitative methods of assessing crystal quality, with an emphasis
on high resolution results.
Q. Polysaccharide crystallization.
R. The trends at the crystallization/diffraction interface - or how big
will a `too small' crystal be in five years.
S. Crystallization in exotic media, including gels.
T. Crystallization of soluble, yet highly hydrophobic, proteins.
U. Problems with oxygen and/or temperature sensitive proteins.
Thanks for your help,
Joe Luft (luft at hwi.buffalo.edu)
George DeTitta (detitta at hwi.buffalo.edu)
Co-Organizers
