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@INPROCEEDINGS{Heigl:827764,
author = {Heigl, Raimund and Stellbrink, Jörg and Radulescu, Aurel
and Schweins, Ralf and Schrader, Tobias Erich and Richter,
Dieter},
title = {{C}hange of {F}ractal {D}imension during the early stages
of{L}ysozyme {C}rystallization},
reportid = {FZJ-2017-01870},
year = {2016},
abstract = {Neutron protein crystallography is a powerful tool to
investigate enzyme mechanisms in depth. It has the advantage
of providing also the hydrogen atom positions which are
practically invisible in x-ray crystallography. Furthermore,
it does not lead to a reduction of the active center due to
radiation damage often encountered using x-rays. Its main
disadvantage is the need for rather large crystals (> 0.5
mm3). This proves to be the biggest bottle-neck when
considering a neutron protein crystallography experiment. To
address this we concentrated on the early stages of the
crystallization process where the directions are set whether
many small crystals grow or few large ones. We used lysozyme
as a model system since it has been studied well in the past
and the phase diagram of its crystal growth is known. We
used a combination of three scattering techniques since the
involved size ranges require a large q-range. Small angle
neutron scattering was used in combination with static light
scattering on the same sample in order to obtain structural
information on the growing crystal seeds. In situ dynamic
light scattering at the neutron scattering sample cell was
used to obtain an overview of all sizes present in the
crystallization process by measuring their hydrodynamic
radii. The small angle neutron scattering technique requires
the crystallization in heavy water instead of normal water.
We found that the crystallization conditions did not differ
too much from the ones mentioned in the literature for light
water when using a corrected pD value of pD=pH+0.4. The
crystallization is initiated by mixing a 60 mg/ml Lysozyme
solution with a 6 $wt\%$ NaCl acetate buffer solution (both
at pD=4.75 and at 298 K) in a 1:1 ratio. Immediately after
mixing, dimers of lysozyme molecules are formed and the
structure factor seen in the lysozyme stock solution
disappears. Under the chosen conditions we could observe a
fractal growth of the crystal seeds with a change of the
fractal dimension from 1.0 to 1.7 in the first 90 min. This
can be interpreted as a crystal seed being formed first
which grows more in a linear manner with little branching.
Later, the space in between the branched arms is filled to
cross over to a more densely packed fractal. With these
results theoretical models of crystal growth can be
improved. Furthermore, the early detection of crystal seeds
can be used to rapidly change the crystallization conditions
(e. g. temperature) in order to avoid the production of more
crystal seeds.},
month = {Sep},
date = {2016-09-20},
organization = {German Conference on Neutron
Scattering 2016, Kiel (Germany), 20 Sep
2016 - 22 Sep 2016},
subtyp = {Outreach},
cin = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
(München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1 /
JCNS-2},
cid = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-2-20110106},
pnm = {6G15 - FRM II / MLZ (POF3-6G15) / 6215 - Soft Matter,
Health and Life Sciences (POF3-621) / 6G4 - Jülich Centre
for Neutron Research (JCNS) (POF3-623) / NMI3-II - Neutron
Scattering and Muon Spectroscopy Integrated Initiative
(283883)},
pid = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6215 /
G:(DE-HGF)POF3-6G4 / G:(EU-Grant)283883},
experiment = {EXP:(DE-MLZ)KWS2-20140101},
typ = {PUB:(DE-HGF)24},
url = {https://juser.fz-juelich.de/record/827764},
}