Small Angle Scattering for Structural Characterization
U-Ser Jeng
Researcher at the National Synchrotron Radiation Research Center
TaiwanAdjunct Professor at the Department of Chemical Engineering
National Tsing Hua University, Taiwan
usjeng@nsrrc.org.tw

Cheiron School 2013, Spring-8 Japan
Sept. 24 – Oct. 3

Contents
Basics of small-angle X-ray/neutron
scattering (SAXS/SANS)
Small/Wide angle X-ray scattering(SAXS/WAXS) instrumentation
Protein solution SAXS

2

Basics of small-angle scattering (SAS)Structure Controls & Civilization
Progressive understanding and Controls of Structures
對結構理解與控制的尺度精度
公分(cm) → 厘米(mm) → 微米(micron) → 次微米(submicron) → 晶體原子結構 (angstrom)
奈米(nm)
The civilization and revolution
當代的文明特徵石器(stone) → 鐵器 (iron)→ 橡膠(plastic) → 矽晶片(semiconductor)電子元件
奈米科技（分子科技）(nanotech. & molecular biology)
Button up structure
Better understanding and controls are motivated by desiring a better life.
But, how to proceed?
4Methodology in Structural Understanding(1) Imaging: light and X-rays (Realspace tools)
TEM, SEM, confocal microscopy, XEM
Field-Ion microscopy(2) Scattering: light, X-rays, neutronsand particles in reciprocal k-spaceor Q-space; exp(ikr-iωt)

0.1 Å

10 Å

1000 Å

Neutron Diffraction

Diffraction for crystal structure (atomic resolution
crystallography, powder diffraction)
Reflection for depth density profile, surface &interface structure of lipid membranes ormonolayers
Small-angle scattering, coherent scattering for noncrystalline structures like proteins in solutions
Inelastic scattering for structural dynamics, phonons
in a liquid crystalline phase

10 µm

Optical Microscopy

Neutron Small Angle Scattering
Neutron Reflection
X-ray Diffraction
X-ray Small Angle Scattering
X-ray Reflection
Electron
Diffraction
Transmission Electron Microscopy

Field-Ion Microscopy

5
scanning Transmission Electron
Microscopy

Interactions of Probing particles and Matter(four types) towards Structural Understanding

Two key factors in selecting probes
Sensitivity (characteristic lengthof the probe)
Penetration power

Revealstructuresfrominteractions

10 Å

1000 Å

6

X-ray scattering probes structures from atomic – molecular(micrometer) structures
Scattered X-rays/neutrons

Understanding scattering
Intensity distributionfunction I(q)Incident X-rays/neutrons

With elastic X-ray/neutron scattering (no energy loss)q = 2k = 4πsinθ/λSAXS/SNAS probes structure in the direction of q, scattering wave vector
2θ : scattering angle

Scattering Intensity distribution profile I(Q)abs
One-dimensional scattering cross section as a function of Q

dσ (Q ) = eik ⋅ rV (r)e − ik '⋅r d 3r 2 = eiQ ⋅ rV (r )d 3r∫∫
dΩ
V (r ) = ∑ j b jδ (r − r j )2V⇒ Scattering Potential (or density distribution of scatterers)iQ • (r −r )i j
I (Q )abs = dσ = ∑ ∑ b b ei jdΩatomic resolution
i j

Bragg diffraction conditions for 2dsinθ = n λQd=2nπQ = 4πsinθ/λbj : Interaction strength or scattering amplitude (length) of the scatterer (cross-section )(electrons for X-ray , nucleus for neutrons), for the probe particles

Small-angle Scattering: at small angles, Q(ri-rj) <<1, summation of each individual atoms
bi is replaced by an integration for a low-resolution density distribution function ρ(r)Experimentally,

I (Q ) ~ ∫ ρ (r )e

−iQ•r

3

d r

molecular resolution(1) Measured scattering intensity distribution, I(Q) ⇒ I(Q)abs(2) From I(Q)abs , deduce electron/nuclide density distribution ρ (r)2General relation between the scattering angle (θ or q) and thecharacteristic length-scale D probed : q (or scattering angle) ~ 1/L

D= 2π/Q

9

For one-component isotropic colloidal system with scattering basic units (form),the SAXS intensity distribution function can be written asiQ • (r −r )i j
I (Q )abs = dσ = ∑ ∑ b b e
i j
dΩ
i j

I (Q ) ~ ( ∫ ρ (r )e − iQ•r d 3r ) 2~
I (Q) = I o P (Q) S (Q)Io : Zero angle scattering intensity (cross section/contrast) I o = CNVp 2 ( ρ scatt − ρ matrix )2
P(Q) : Normalized particle structure factor, determined by2
size and shape of scattering particles P(Q ) = ∫ ρ (r )e −iQ•r d 3r
S(Q) : inter-particle structure factor; determined by particle
distribution (i.e. pair-correlation function).
C: concentration of scattering particles
N: aggregation number (=1 for no aggregation)
Vp: dry volume V for the scattering particles
ρscatt: scattering length density of the scatter(scatter density and scattering length summed from all atoms)ρmatrix: scattering length density of the matrix

SAXS can differentiate size and shape in a nanometer scale
P(Q ) = ∫ ρ (r )e −iQ•r d 3r

210

 Sphere~2
P (Q ) = (3 j1 (QR ) / QR )j1 ( x ) = (sin x − x cos x ) / x 2
 Ellipsoidav = [a µ + b (1 − µ )]µ = cosθ

R
L

2

2

2

1/ 2

b

Rod or1 disk2
2 J 1 (v) sin( w)~
P (Q) = ∫dµvw
0

Rod (L=80 Å, R=20 Å)
Disk (T=40 Å, R=40 Å)

1

0.1

P(Q)

3 j1 (v)~
P (Q) = ∫
dµ
v
0
2

θ

2

1

Ellipsoid (a=40 Å, b=20 Å)

0.01

0.001
Sphere (R=20 Å)
Sphere (R=40 Å)

0.0001R

T J (v): first order Bessel function
1

v = QR(1-µ2)1/2 ; w = 1/2QTµ

0.00

0.05

0.10

0.15

Q (Å-1)

0.20

Q = 4πsinθ/λRadius of gyration Rg for particles of irregular shapes - Guinier
approximation (Qr <<1; expansion of exponential term )P(Q ) = ∫ ρ (r )e −iQ•r d 3r

Rg

2

Particles of irregular shapes (then ignore shape for size only; ρ = constantI (Q ) ≈ I o exp( −Q 2 Rg2 / 3)

Qx 2 X 2 + Qy 2Y 2 + Qz 2 Z 2 ≈ 1 / 3Q 2 R 2ln(Q) = -(1/3)Rg2Q2-1

Rg: Radius of gyration-2

R g = ∫ ρ ( r ) r dV / ∫ ρdV
2

For spheres of uniform density ρ

R = 4πρ ∫ (r 2 )r 2 dr /( ρV ) = (3 / 5) R 2
2
g

R
0

Rg and scattering shape !!

ln(I(Q))(Guinier approximation is valid when QRg <<1 )C60-ionomer aggregate
4 % (Rg= 21.7 Å)
1 % (Rg= 19.2 Å)

-3

-4

-5

slope = - Rg2/3

-6
0.000

0.005

0.010
2

-2

Q (Å )

0.015

Scatteringfeaturesvs.
Shape
P(Q ) = ∫ ρ (r )eRadius of gyration Rg for all
shapes of particles,
especially spheres−iQ •r3d r

Kratky-Porod approximation for the radius or
thickness of rod-like or disk-like particles

2

Guinier Approximation

For spheres of radius R

For cylinders of radius R

For disks of thickness t

For one-component isotropic colloidal system, the SAXS intensity
distribution function can be written asiQ • (r −r )
~
i j
d
σ
I (Q )abs == ∑ ∑b b e
I (Q) = I o P (Q) S (Q)
i j
dΩ
i j
Io : Zero angle scattering intensity I o = CN ( f − ρ wVp )2

P(Q) : Normalized particle structure factor, determined bysize and shape of the scattering particles
S(Q) : inter-particle structure factor; determined by particle
pair-correlation function (particle distribution).

Ordered arrangement of scattering particles inspace - Structure factor S(Q)
Colloidal solution containing monodisperse particles: I (Q) = npP(Q)S(Q)
np = N/Vs : Number density of particles
P(Q) : ∫vρ(r)d3r, Particle form factor (intra-particle interference)
S(Q) : Structure factor (interference between scattering particles)iQ ⋅ (R −R )
j
i
1 N N
S (Q ) =
∑ ∑ e
N i j
∞

= 1 + n p ∫ 4πr 2 ( g ( r ) − 1)(sin(Qr ) / Qr )dr0g(r) = (1/<ρ(r)>2)∫ρ(r')ρ(r'-r)d3r ⇒ pair correlation function[s(0)]-1 = (1/kbT)(∂Π/∂np) = 1 + 2 B2np ; (related to compressibility)
B2 ⇒ the second Virial coefficient

15

Structure factor S(Q) for hard spheres∞

S (Q ) = 1 + n p ∫0 4πr 2 ( g ( r ) − 1)(sin(Qr ) / Qr )drg(r) = Pair correlation function for the nanograins (excluded volume effect)
Hard sphere : S (Q ) = 1 /[1 − npC (Q )]Size growth with
3 (sinξ−ξcosξ) +1.2a constant shape
C(Q) = 4πσ3ξ−6
{α
ξ
o
0
2.0
10
QC = 0.0272 Å
o 1.1
2
2
η =of
0.092, R = 15 nm
105C
Ordering
β oξ [2ξsinξ−(ξ −2)cosξ−2] + γoη = 0.092, R = 11 nm
95 C1.0
3
4nanograins[(4ξ −24ξ)sinξ−(ξ −12ξ+24)cosξ+24]}
η = 0.092, R = 5.5 nm
gg

0.91.50.00

0.05• η : Volume fraction (= npV)of PFO nanograins• Domain distance D ~ (np)-1/3

0.10

Q (Å-1)

P(Q) (R=20 Å)

0.8

S1(Q), η = 0.10, σ =40ÅS2(Q), η = 0.05, σ =40ÅS3(Q), η = 0.01, σ =40Å

0.7

I (Q)
S(Q)

σ : the effective
10-1 diameter,ξ = qσ,αo = (1+2φ)2(1−φ)–42(1−φ)–4β o = –6φ [1–(φ/2)]
a=8.8~10.2 nm
10-2
γ = φαo/2b=2.8~3.3 nm
φ :the effective volume fractiong0.61.00.5

I1(Q) =P(Q)S1(Q)0.4
2b (8 nm)
0.5

I2(Q) =P(Q)S2(Q)I3(Q) =P(Q)S3(Q)

0.3
0.2

0.15

2a (20 nm)

0.1
0.20
0.0
0.0 0.00
0.00

0.05

0.05

0.10

0.10

0.15
Q
(Å-1) 0.20

Q (Å-1)

0.15

0.25

0.30

17

S(Q) for more ordered structure
Self-assembly of block copolymers for meso-scale (10-100 nm)
ordered structures
1000

S(Q):ordering of domains
Q-ratio of the scattering peaks(1) Periodic structure：
1 : 2 : 3 : 4…;(2) Body-centered cubic array：
1: √2 : √3 : √4 : √5 …. ;(3) Hexagonal array
1: √3 : √4 : √7 : √9 : √12q*oPS-b-PEO copolymer

30 C
o
60 C
o

100

80 C
o
100 C
柱 狀P(Q )31/2q*
1/2
4 q*

10

I (cm-1)

P(Q):domain size, shape(sphere, rod,cylinder, etc..)
N

1/2
12 q*

1

0.1

0.01
0.01

0.1

Q (Å-1)17

0.2

Extract form factors of NPs & copolymer block from a
copolymer/NP composite
Copolymer PS-b-P4VP/Nanoparticles complex— ordered
meso-scale phase separation
1000
7% CdS/S4VP
P(Q)
100
200nm

P1(Q) for CdS
S(Q)fitted S(Q)

10

I (Q)

P(Q):domain size, shape
12 nm P4VP
Slabs + 3.5 nm CdS
N
dispersed nanoparticles
S(Q): ordering of domains
散射峰的 Q 值比例， 1 : 2 : 3
層板週期性的排列結構特徵

1Ordered domain size
estimatedfrom scattering peak width
Sherrer eq. with SAXSLong period =2π/Q
D ~ 2π/∆Q∆Q : Full width half maximum

0.1

Complementary between
TEM (real space) &Scattering (q-space)

0.01
0.01

0.05

0.10

Q (Å-1)18

What can be learned from protein solution SAXS:Fold structure and charge interactions of lysozyme~
I (Q) = I o P (Q) S (Q)Ellipsoidal
form factor
1

Lysozyme interacts through ascreened charge potential V(r)of long range interaction insolutions.
V(r) ⇒ g(r) ⇒ S(Q)MSA Structure
factor
S(Q)

P(Q)

I(Q) (cm-1)− k ( x −1)V ( x) γe − k e,=xk BT  ∞
,


x >1
x ≤1

γe

−k

4( Ze) 21=
k B T εσ (2 + k ) 2

0.1

Structural parameters
extracted from data fitting
0.01

42 mg
21 mg
10.5 mg
7mg

0.00

0.05

0.10
Q (Å-1)

0.15

0.20

Ellipsoid shape (a=31 Å, b=14Å)Rg = 16.6 Å
S(Q) is consistent with 6 net
positive charges on surface
19Fractal aggregation of hydrophilic fullerenederivatives C60(OH)18 in aqueous solution
Pair correlation function

g (r ) ∝ r
N*

D −d

exp(−r / ξ )10
斜 率 = - 2.5 (D = 2.5)

S(Q) for fractal structure

P(Q) ~ 1 ⇨I(Q) =P(Q)S(Q)~S(Q)C (wt %)

I(0) (cm-1)

Rg (Å)

Rg* (Å)

ξ (Å)

0.625

0.21

22.4 ± 3.0

28.3

1.25

0.39

25.6

2.5

1.04

26.9

N

N’

13.4

48

40

31.7

15.0

55

54

37.2

17.6

74

80

4.0

3.21

34.3

44.2

20.9

113

125

*10.0

5.18

−

37.4

17.7

−

−

-1

1
DΓ( D − 1)
−1
sin[(
1
)
tan
(Qξ )]
D−( D −1) / 2
D2−
Q (1 + (Qξ ) )I (cm )S (Q ) ~

1

0.1

0.01

C60-OH18 ∼2ξ
4 wt% (ξ=20.9 Å)
2 wt% (ξ=17.6 Å)
1 wt% (ξ=15.0 Å)

0.001
0.01

0.1

Q (Å-1)
20

0.2

0.3

Dummy residues simulation package for protein
unfolding structure
SAXS data for lysozyme
1

Protein pair correlation function

21 mg Lysozyme/8M urea, in buffer solution of pH = 2.9, 0.1 M NaClo

Ellip. a=25.9 , b=14.5Å

o

50 C

Ellip. a=38.3 , b=17.0Å

60 oC

Ellip. a=44.5 , b=17.0Å

30 C

Gnom package

I(Q) (cm-1)

0.1

0.01

Cool back to 30 oC

Ellip. a=32.0 , b=14.5 Å

0.001
0.00

0.05

0.10

0.15

0.20

Q (Å-1)Re-calculate SAXS profile

CRYSOL +modified PDB

Fit p(r) using Gsbor package
Cα Bound water
based on dummy residues

21• GNOM Program

Transform data to distance distribution function p(r) with GNOM program and dodata fit.
Distance distribution functions oftypical geometrical bodies.

PmrA, Dmax = 105 Å

merged profile
PmrA

I(q) (cm-1)

0.01

1E-3

1E-4

1E-5
0.1

-1

q (Å )

22

Dmitri I Svergun and Michel H J Koch, EMBL Rep. Prog. Phys. 66 (2003) 1735

Available on-site DATA simulation kit
with ATSAS developed by the EMBL group
ATSAS 2.5.1 (analysis software)With PDB file
BL23A
On-siteDATA
Simulation

VMD (molecular graphics software)23

3. Data analysis and Model simulation
 Crysol fitting
Compare (fit) solution structure with PDB crystal structure.
•

Open the log file to read theexperimental and theoretical Rg values
and 7.08

24

 Dammin Program
An ensemble of dummy atom model simulation with P(r) output by GNOM.

Dammin

Displayed by VMD

Final SQRT(Chi) against raw data: 1.069

GASBOR Output Files:
1. log file: contain the same information as the screen output.
2. fir file: fit to the raw experimental data
3. pdb file: resulting model in PDB-like format that can be viewed with MASSHA (in ATSAS package) or VMD (molecularvisualization program)25

 Gasbor Program
An ensemble of dummy residues model simulation with P(r) output by GNOM.

Gasbor

Simulation by Gasbor

PDB structure
Final Chi2 against raw data .......... : 14.508
Final Chi2 against corrected data . : 1.874

GASBOR Output Files:
1. log file: contain the same information as the screen output.
2. fir file: fit to the raw experimental data
3. pdb file: resulting model in PDB-like format that can be viewed with MASSHA (in ATSAS package) or VMD (molecularvisualization program)

26

Fitting SAXS data with SASref for relative orientation of
two-domain proteins of respective PDB files(CY Chen et al., NSRRC)

Protein Solution SAXS

10-1

5.65 nm

pH =9

10-2

I(q) (cm-1)

CBP21

3.19 nm

NCTU2

10-3
CBP21-(EAAAK)5-NCTU2 (pH9)iEXP
Sasref (χ=2.69)
10-4
0.01

0.1
q (Å-1)

Data processing

Data analysis
and simulation

28

Unfolding of Lysozyme

29

EMBL Hamburg BioSAXS team effort in ATSAS software package.
The data analysis software can be downloaded fromhttp://www.embl-hamburg.de/biosaxs/atsas-online/download.php
user forum for software problems
http://www.saxier.org/forum/viewforum.php?f=530

Introduction of small angle X-ray
scattering (SAXS)
Synchrotron small/wide angle X-ray
scattering (SWAXS) instrument
SAXS activities at the NSRRC

31

Introduction of
X-ray source for scattering32

Traditional X-ray Source• Single characteristic wavelength• Flux~ 106 photons/s
33

Synchrotron Radiation X-ray Source

Advantages of using Synchrotron Radiation X-ray• High Flux 3x1011 photon/s (time-resolved measurement)• Tunable wavelength (anomalous scattering for multiphase structure)34

JapanHsinchu

China

TaiwanPhilippines

35

2014
Commissioning of Taiwan Photon Source

Taiwan light source TLS (1.5 GeV; 120 m)

Taiwan photon source TPS (3.0 GeV, 548 m)

36

同步加速器聚頻磁鐵光亮度比較(TLS, SLS, Diamond, SPring-8, TPS)

Brilliance (Phot/s/0.1%bw/mm2/mr2)

1022

TPS_LSU15
TPS_IVXU28

1021

TPS_EPU46

1020

SP8_IVXU32
TPS_U1001019

SLS_UE56
TLS_EPU56

Diamond_U31

1018
TPS_SW60

1710

TLS_U91016>1,000,000 folds enhanced brilliance
TLS_SW60

3 GeV, 400 mA
1.5 GeV, 400 mA

1015
101

102

103

Photon Energy (eV)

104

105
37

Synchrotron SAXS
instrumentation

38

The newly installed BL23A SAXS beamline
Low beam divergenceWide energy range
High flux and high energy resolution
deflectable beam
3.1 T
(1:1 focusing)BL23A SWAXS beamline:
Energy Resolution/Photon Flux regulated by the DCM/DMM
Si(111)
Crystals
DCM mode(4.9-23° for 5-23 keV)
X-raysMultilayer
OpticsCrystal 1

DMM mode(0.9-2.4° for 7-13
6-15 keV)
keV
X-raysMultilayer 2

Crystal 2

X-ray

Multilayer 1

The inner structure of DCM/DMM monochromator.
40

1013

∆E/E

6

30

4

20

2

10

0

0
5

1012

10

(b)

40

IR

15

E (keV)

1011

Flux of
DCM/DMM
monochromatizd
beam

DMM
DCM

1010

Beam position shift (µm)

1014

8

Beam shift at the sample
position due to the
100DCM/DMM
exchange of
IR

1015

-2

1016

∆E/EDMM (10 )Flux Density (photons/s/300 mA)

Performance of DCM/DMM
VerticalHorizontal

50

0

-50

109
-100

108
5

10

15

20

25

5

30

15

Photon Energy (keV)

Photon Energy (keV)

Crystal type10

Dimensions
(mm3)

DCM

Si(111)

1st : 50×20×3#
2nd : 50×40×40

DMM

Mo/B4C(200 layers)(L×W×H)
190×30×33

E (keV)∆E/E

θ (°)*

Flux (photons/s)+

5-23

2-5×10-4

4.9-23109 - 1010

6-15

1.1×10-2

0.9-2.4

1-4×1011
41

The SWAXS (synchronized SAXS & WAXS) instrument at
BL23A1 Endstation of the NSRRC

Beam stop

2-D detector

WAXS

Q
SAXS

Master 2-D detector (SAXS) slaves the linear detector (WAXS)
42

Highly automatized BL23A SWAXS instrumental the NSRRC
Collimation stageSample stage
Automatic Bellow systemfor continuous changes in S-D distance under vacuum
Interchangeable
CCD/gasdetectors
for SAXS

Two linear detectors
for WAXS

Liu, D. G. et al. J. Synchrotron Rad., 2009, 16, 97.
Jeng, U. et al. J. Appl. Cryst. 2010, 43. 110
43Feb. 25-26, 2013
Tokai Japan
23A SWAXS
Detecting System

Flat Panel (2D WAXS)
X-raysMythen 3K(WAXS-V)

1D Gas Detector(WAXS-H)

MarCCD (SAXS)

Pilatus 1M-F (SAXS)SAXS Dets (1100 – 5000 mm)

Flat Panel (90 – 200 mm)

NSRRC BL23A Small/Wide-Angle X-ray Scattering
1D Dets (400 – 1000mm)

Sample Stage (0 mm)
44

Front View/Back View

Computer controlled sample-to-detector distance(1 – 5 m) with vacuum bellow system
X-ray beam energy
6- 15 keVFor detectable
protein (complex)
morphologyof 1 – 100 nm size
45

Integrated Triggering System for milli-second SAXS/WAXS
Activated by SAXS detecting sys.

Det. System witching board
Synchronizing center
1.CCD system; 2.SPEC/Pilatus system

To WAXS Det. sys.

To Sample System:
Stopped flow, T-jumptemp control, stress devic

To analytical instru.
: DSC; UV-vis abs.
strain recording,viscosity recording;46Current Detectors
Pilatus 1M-F

Mythen 1k *3

Flat Panel

Pixel size

172 μm

50 μm

50 μm

Format981 x 1043

1280 x 3 (Linear)

1032 x 1032

133 Hz472 Hz3.3 HzSAXS

1D WAXS

2D WAXS

Frame Rate

47

NSRRC BL23A SWAXS Endstation
Pinhole/slits system

Collimation stage with 2 pin-hole slit sets

Detector systems
SAXS area
detector
1.5 – 5 m
2 liner WAXS det.
0.3 – 1 m

48

Sample environments for correlations between
structure and property
SAXS/WAXS/DSC

Linkam TST350 tensile stress tester

PVC/PBA blend film

Linkam CSS450 shear stage

In-situ LN2 gas cooling process from320-243 oC
Syndiotactic Polystyreneo (Tg = 100 oC,
Cooling rate 200 C/min
Tm = 270 oC)o

Or water cooling >100 C/s

Performance for simultaneous ms-SAXS/WAXS for structural evolution
The simultaneous SAXS/WAXS measurements of the melt-crystallization process from
200oC to 86oC of isotactic polypropylene (500 ms resolution).
(Applicable to protein crystallization processing?? morphology change before
crystallization)。

Pilatus

MythenW.R. Wu, et.al. ACS Nano 5 , 6233, 2011
10000
1000

z
1000

100

100

10

10

1

0.1

0.01

x

GISAXS
for
PCBM aggregation

qz (Å-1)

1

0.1
0.01

GIWAXSfor
P3HT
crystallization
GISAXSgg

2D-GISAXSGISAXS
Area Detectorqz

qx (Å-1)

2D-GIWAXSGIWAXS
Area Detector

qz

qx

β
Φ

Sample

X-ray

α

qx

BHJ Solar cell performance
test

Forming
Percolated/Mutually
Confined Fullerene vs.
Polymer Nanograins in
BHJ Solar Cells

Unique Opportunity with the new SWAXS instrument— GISAXS for nanostructures on liquid surfaces
For liquid surfaces

Grazing Incident scattering
GISAXS/GIWAXS
for liquid surfaces
for in-plane structure

I(Q⊥)

I(Q||)
Scattered beam

Total reflected beam
Incident X-ray

X-raysLangmuir Trough

By N. Torikai52

At 25 oC: Lamellar-to-H2D route (GISAXS)

Molar ratio: H2O : HCl : CTABr (61 mM) : TESO = 100: 2: 0.11 : 0.16(2a)t=1200 s

0.5

0.4

0.4

0.3

0.3

0.2

0.2

0.1

0.1

0.0

0.0
-0.2

-0.1

0.0

qx (Å-1)

0.1

0.2

(2b)

t=2820 s
03

02

01

0.5

(2c)

t=6540 s

0.4

Qz (Å-1)

qz (Å-1)

0.5

0.3
0.2
0.1
0.0

-0.2

-0.1

0.0

qx

(Å-1)

0.1

0.2

-0.2

-0.1

0.0

qx

(Å-1)

0.1

0.2

53

SAXS working with complementary tools forProtein folding-unfolding
X-ray

Cyt c
Four-mixing stopped-flow device for in situ
reactions / SAXS

urea
ctyc

Buffer0.1

GdHCl

I(Q) (cm-1)

X-ray
native 300
u8M 300
1:7 (7M) 300
2:6 (6M) 300
0.5:7.5 (7.5M) 300
1.5:6.5 (6.5M) 300
3:5 (5M) 300

0.01

0.001

0.05

0.10

0.15

0.20

0.25

0.30

0.35

Q (Å-1)
sample area
capillary tubing

In-situ SAXS for protein titrated
with denaturant solutions

Progress at 23A endstation

Stacking/fusing kinetics of positively-negatively charged lipid membranes
revealed by 10-ms-resolved SAXS with stopped-flow system
Four-mixing stopped-flow device for in situ
reactions / SAXS++++ Lipid bicelles - - - Condition
15% Charge 10mM
DC-Chol/DPPG mix 3:7
No. 070~150 frame
10 ms/frame

Click for Moviein situ membrane fusion
X-ray

0~1 photon/pixel/10 ms
Stacking ordering peak
Frame number
10 ms/frame
1-3
0-9
10-19
20-29
40-49
60-69
80-89
190-199390-399790-799
980-989

I(Q) (cm-1)

0.06

sample area
capillary tubing

0.03

0.00
0.08

0.10
-1

Q (Å )

0.12

M. Nakano et al.
0.0042

15% Charge 10mM DC-Chol/DPPG mix 3:7

0.00400.0038Intensity (a. u.)

0.00360.00340.00320.00300.00280.00260.00240.0022
-60

-40

-20

0

20

40

60

80

100

120

140

160

0.011

time (ms)Mechanism of membrane fusion
and lipid exchange

Intensity (a. u.)

15% 10mM DC/DPPG mix 3:7

0.010

0.009

0.008

1

10

Time (sec)

100

WAXS

SAXS
SAXS/WAXS
for food forsciencein tuningtexturefor digestion,
Simultaneous
SAXS/WAXS
food scienceat food
the BL23A
SWAXS
Endstation preservation, or taste

Green beam Noodle- pure starch (冬粉)

Wheat Noodle(麵線)
textureSpaghetti, Italy-Noodle(直條義大利麵)

WAXS

looking for gourmet
food texture

SAXS
by U-Ser Jeng, Wei-Ru Wu & Kuei-Fen Liao, Nov. 26, 2011

Rice-Noodle – pure starch (米粉)Ice Cream (松子冰淇淋)after melt and re-frozen

SAXS/WAXS for
Carbohydrate Polymers: starch
granules100

Surface fractal dimension (ds):
Ice cream ds =2.5
Re-frozen ice cream ds = 2.9

10

Wheat noodle ds =2.4
Spaghetti ds = 2.7

10

Intensity

Intensity

q-3.1
q-3.5

1

100

Wheat thin noodle (? ? ) (~10% starch)
Spaghetti (14% wheat starch based)

q-3.3 q*

1

2q*

q-3.6
0.1

0.1

d = lamellar spacing
Ice cream d =3.9 nm
0.01 Re-frozen ice cream d = 3.8 nm
0.01

0.01

Wheat noodle d =10.7 nm
Spaghetti d = 10.3 nm

q-3.3

1

q-3.2

0.01

0.1

No lamellar structure
0.01

0.1

q (A-1)q (A-1)6000

A-type starch

Ice Cream
Melt/re-frozen Ice Creamq (A-1)

Wheat Noodle
Spaghetti

6500

B-type starch

8000

5500

7500

Intensity

4500

Green beam Noodle
Rice Noodle

7000

6000

Enhanced Ice ring

5000

Intensity

Intensity

Green beam noodle ds=2.7
Rice noodle ds = 2.8

0.1

0.01

0.1

Green Beam noodle (~50% starch)
Rice noodle (10~20% starch)

10

Intensity

Ice-Cream
Re-Freezed Ice-Cream

100

5500

6500
6000
5500

5000

4000

5000
3500
1.0

1.2

1.4

1.6

1.8
-1

q (Å )

2.0

2.2

2.4

4500
0.4 0.6 0.8 1.0 1.2 1.4 1.6 1.8 2.0 2.2-1

q (Å )

2.4

Inulin (菊糖: 膳食纖維)

4500
0.4

0.6

0.8

1.0

1.2

1.4

1.6
-1

q (Å )

1.8

2.0

2.2

2.4

Prof. Ying-Huang Lai (賴英煌) and his teamDr. Yi-Qi Yeh (葉奕琪)Team members /Collaborators

 SAXS group members: Chun-Jen Su, Dr. (蘇群仁; 23A beamline manager); Yi-Qi Yeh (葉奕琪); Liao, Kuei-Fen (廖桂芬); Wen-Bin Su (蘇文斌); Wei-Ru Wu (吳瑋儒); Collaborators: Drs. Wei-Tsung Chung (莊偉綜)， Yu-Sang Huang (黃玉山), Ming-Tao Lee(李明道), Chun-Yu Chen (陳軍佑); Prof. Ying-Huang Lai (賴英煌); Dr. Chiu Hun Su (蘇秋琿),Prof. A. C. Su (蘇安仲); I-Chi Huang (黃彥之);~ Thank you
for your attention~
Dr. Chun-Jen Su (蘇群仁)
Ms. Liao, Kuei-Fen (廖桂芬Dr. Chiu Hun Su (蘇秋琿)