Growth
inhibition of protein crystals: A study of lysozyme polymorphs
Author(s): Heijna MCR, van Enckevort
WJP , Vlieg E
Cryst. Growth & Des. 8 no. 1
(2008) 270-274
Abstract:
Crystal morphology is determined by the relative growth rates of the
different faces involved. Opposite faces (hkl) and (hkl) can show
different rates if the crystal structure does not have inversion
symmetry. Protein crystals, being built of asymmetric molecules, do not
have identical opposite faces, except for those pairs linked by
rotational symmetry. Here, we present an in situ microscopy study on
the polar growth of various polymorphs of hen egg-white lysozyme
crystals. It was found that in a number of cases the growth of one of
the two faces was blocked, whereas the opposite one was not slowed
down. To explain our results, we propose a self-poisoning mechanism
based on solvent-induced adsorption of misorientated lysozyme molecules
on the inhibited faces. This mechanism can also prevent some proteins
from forming crystals at all.