Impact of Diffraction Data Volume on Data Quality in Serial Crystallography
Crystals,
Год журнала:
2025,
Номер
15(2), С. 104 - 104
Опубликована: Янв. 21, 2025
Serial
crystallography
(SX)
enables
macromolecular
structure
determination
at
biologically
relevant
temperatures
while
minimizing
radiation
damage.
This
technique
relies
on
processing
numerous
diffraction
images
from
multiple
crystals
to
construct
a
complete
dataset
for
three-dimensional
determination.
Although
increasing
the
volume
of
SX
data
improves
quality,
excessive
collection
reduces
beamtime
efficiency.
Therefore,
understanding
relationship
between
and
quality
is
crucial
efficient
use
beamtime.
In
this
study,
serial
synchrotron
datasets
lysozyme
glucose
isomerase
were
analyzed
assess
impact
varying
volumes
statistics
structural
outcomes.
Data
refinement
metrics
improved
as
integrated
increased;
however,
rate
improvement
in
was
not
proportional
number
patterns.
Furthermore,
decreased
beyond
certain
threshold
volume.
These
findings
expand
our
provide
insights
into
optimizing
efficiency
processing.
Язык: Английский
Temperature-Dependent Structural Changes of the Active Site and Substrate-Binding Cleft in Hen Egg White Lysozyme
Crystals,
Год журнала:
2025,
Номер
15(2), С. 111 - 111
Опубликована: Янв. 22, 2025
Lysozyme
plays
a
crucial
role
in
the
natural
immune
system,
protecting
against
invading
bacteria
or
viruses.
The
room-temperature
(RT)
structure
of
lysozymes
is
important
for
understanding
accurate
structural
information
compared
to
crystal
determined
at
cryogenic
temperature.
Several
RT
structures
are
by
serial
crystallography,
but
their
temperature-dependent
properties
not
fully
elucidated.
To
better
understand
change,
and
temperature
hen
egg
white
lysozyme
(HEWL)
were
synchrotron
crystallography
(SSX)
macromolecular
(MX),
respectively.
Structural
comparisons
HEWLRT
HEWLCryo
showed
that
positions
loops
above
substrate-binding
cleft
HEWL
differed.
width
between
α-
β-domains
was
wider
than
HEWLCryo.
distance
two
catalytic
residues
Glu53
Asp70
interaction
with
neighbor
water
molecules
distant
Due
temperature,
subtle
movements
active
site
led
different
docking
results
N-acetylglucosamine
N,N′,N″-triacetylchitotriose.
These
will
provide
useful
more
accurately
molecular
function
insights
into
effects
ligand
design.
Язык: Английский
Temperature-Dependent Structural Changes in Xylanase II from Trichoderma longibrachiatum
Carbohydrate Research,
Год журнала:
2024,
Номер
541, С. 109173 - 109173
Опубликована: Май 31, 2024
Язык: Английский
Recognition of a Single β-D-Xylopyranose Molecule by Xylanase GH11 from Thermoanaerobacterium saccharolyticum
Crystals,
Год журнала:
2024,
Номер
14(5), С. 402 - 402
Опубликована: Апрель 26, 2024
The
endo-β-1,4-xylanase
glycosyl
hydrolase
(GH11)
decomposes
the
backbone
of
xylan
into
xylooligosaccharides
or
xylose.
These
enzymes
are
important
for
industrial
applications
in
production
biofuel,
feed,
food,
and
value-added
materials.
β-D-xylopyranose
(XYP,
also
known
as
β-D-xylose)
is
fundamental
unit
substrate
xylan,
understanding
its
recognition
initial
steps
GH11’s
molecular
mechanism.
However,
little
about
a
single
XYP
molecule
by
GH11.
In
this
study,
crystal
structures
GH11
from
Thermoanaerobacterium
saccharolyticum
(TsaGH11)
complexed
with
an
were
determined
at
resolution
1.7–1.9
Å.
binds
to
subsite
−2
substrate-binding
cleft.
mainly
stabilized
π–π
interaction
conserved
Trp36
residue.
O2
O3
atoms
hydrogen
bond
interactions
hydroxyl
groups
Tyr96
Tyr192.
conformation
thumb
domain
TsaGH11
does
not
play
critical
role
binding,
binding
induces
shift
toward
molecule.
A
structural
comparison
other
xylanases
revealed
that
forms
stacking
center
between
phenyl
indoline
ring
Trp36,
whereas
xylobiose
xylotetraose
which
indicates
modes
differ.
results
provide
greater
family.
Язык: Английский
Single pulse data collection with an X-ray chopper at in situ room temperature Laue crystallography beamline BL03HB
Nuclear Instruments and Methods in Physics Research Section A Accelerators Spectrometers Detectors and Associated Equipment,
Год журнала:
2024,
Номер
unknown, С. 169891 - 169891
Опубликована: Сен. 1, 2024
Язык: Английский