Annular beam high-intensity X-ray diffraction based on an ellipsoidal single-bounce monocapillary

2016 ◽  
Vol 49 (2) ◽  
pp. 627-631 ◽  
Author(s):  
Fangzuo Li ◽  
Zhiguo Liu ◽  
Tianxi Sun
Keyword(s):  
High Intensity ◽  
Focal Spot ◽  
Crystallographic Analysis ◽  
Field Pattern ◽  
X Ray Diffraction ◽  
Ccd Imaging ◽  
X Ray ◽  
Imaging Detector ◽  
Sequential Image ◽  
Sequential Images

This short communication presents a study of the use of an annular X-ray beam produced by an ellipsoidal single-bounce monocapillary (ESBC) to perform focal construct geometry (FCG) high-intensity angular-dispersive X-ray diffraction (ADXRD) in transmission mode. The ESBC optic effectively focused a large focal spot X-ray source into a smaller focal spot and produced a narrowed X-ray ring in the far-field pattern when combined with a beam stop. A CCD imaging detector was linearly translated along the principal axis of the ESBC-FCG and obtained the corresponding sequential images of diffraction concentric circular caustics and convergence points, which were formed by the constructive interference of a continuous set of Debye cones arising from the annular interrogation volume. Pixels from the central region of an approximately 0.6 mm2 area were interrogated on each sequential image; as a result, a one-dimensional diffractogram of an aluminium oxide sample was revealed. The presented ESBC-FCG ADXRD technique shows potential for increasing the diffracted intensity and streamlining the operation of crystallographic analysis.

scholarly journals A putative siderophore-interacting protein from the marine bacteriumShewanella frigidimarinaNCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis

2016 ◽  
Vol 72 (9) ◽  
pp. 667-671 ◽  
Author(s):  
Inês B. Trindade ◽  
Bruno M. Fonseca ◽  
Pedro M. Matias ◽  
Ricardo O. Louro ◽  
Elin Moe
Keyword(s):  
Iron Acquisition ◽  
Crystallographic Analysis ◽  
Monoclinic Space Group ◽  
Molecular Replacement ◽  
X Ray Diffraction ◽  
Interacting Protein ◽  
X Ray ◽  
Cell Parameters ◽  
Unit Structure ◽  
Shewanella Frigidimarina

Siderophore-binding proteins (SIPs) perform a key role in iron acquisition in multiple organisms. In the genome of the marine bacteriumShewanella frigidimarinaNCIMB 400, the gene tagged as SFRI_RS12295 encodes a protein from this family. Here, the cloning, expression, purification and crystallization of this protein are reported, together with its preliminary X-ray crystallographic analysis to 1.35 Å resolution. The SIP crystals belonged to the monoclinic space groupP21, with unit-cell parametersa= 48.04,b= 78.31,c= 67.71 Å, α = 90, β = 99.94, γ = 90°, and are predicted to contain two molecules per asymmetric unit. Structure determination by molecular replacement and the use of previously determined ∼2 Å resolution SIP structures with ∼30% sequence identity as templates are ongoing.

X-ray diffraction has limited applicability in investigation of milk tampering

2019 ◽  
Vol 86 (3) ◽  
pp. 337-340
Author(s):  
Ana Paula Pavão Battaglini ◽  
Alexandre Urbano ◽  
Vanerli Beloti ◽  
Edson Antonio Rios ◽  
Juliana Ramos Pereira ◽  
...  
Keyword(s):  
Sodium Citrate ◽  
Freezing Point ◽  
Raw Milk ◽  
Physicochemical Analysis ◽  
Crystallographic Analysis ◽  
X Ray Diffraction ◽  
Water Addition ◽  
X Ray ◽  
Freeze Dried ◽  
Limited Applicability

AbstractThe aim of this work was to use X-ray diffraction to identify substances used for adulteration of raw milk and to determine if crystallographic analysis can detect extraneous substances in milk. Two unknown substances were sent anonymously by employers linked to the dairy chain, who claimed that they were added directly in milk prior to water addition by truck drivers. The samples were analyzed by X-ray diffraction and submitted to physicochemical analysis. The first substance was identified by X-ray diffraction as sodium citrate, complying with its physicochemical attributes, such as the powerful ability to decrease the freezing point. The second substance was identified by X-ray diffraction as sucrose and this result was also in agreement with its ability to increase the density, decrease the freezing point and finally, to be positive for sucrose in the resorcinol qualitative test. To evaluate if X-ray diffraction can detect extraneous substances already mixed in milk, fresh raw milk samples tampered with urea, sodium hydroxide, sodium citrate and sucrose were freeze dried and analyzed by X-ray diffraction, with no detection of any extraneous substances at any percentage. This is the first report of attempted diagnosis of extraneous substances in milk by X-ray diffraction. However, this technique can be useful only when applied to identify substances used for adulteration prior to its dilution in milk, since the amorphous nature of milk seems to be a limitation for the accurate detection of extraneous substances.

scholarly journals Crystallization and preliminary crystallographic analysis of manganese lipoxygenase

2014 ◽  
Vol 70 (4) ◽  
pp. 522-525 ◽  
Author(s):  
Anneli Wennman ◽  
Ernst H. Oliw ◽  
Saeid Karkehabadi
Keyword(s):  
Expression System ◽  
Crystallographic Analysis ◽  
Gaeumannomyces Graminis ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Parameters ◽  
Apparent Homogeneity ◽  
Structural Differences ◽  
Position Specificity ◽  
Take All

Lipoxygenases constitute a family of nonhaem metal enzymes with catalytic iron or, occasionally, catalytic manganese. Lipoxygenases oxidize polyunsaturated fatty acids with position specificity and stereospecificity to hydroperoxides, which contribute to inflammation and the development of cancer. Little is known about the structural differences between lipoxygenases with Fe or Mn and the metal-selection mechanism. APichia pastorisexpression system was used for the production of the manganese lipoxygenase of the take-all fungus of wheat,Gaeumannomyces graminis. The active enzyme was treated with α-mannosidase, purified to apparent homogeneity and subjected to crystal screening and X-ray diffraction. The crystals diffracted to 2.6 Å resolution and belonged to space groupC2, with unit-cell parametersa= 226.6,b= 50.6,c= 177.92 Å, β = 91.70°.

scholarly journals Crystallization and preliminary X-ray crystallographic analysis of carboxyl-terminal region 4 of SigR fromStreptomyces coelicolorA3(2)

2014 ◽  
Vol 70 (6) ◽  
pp. 747-749
Author(s):  
Keon Young Kim ◽  
Sunmin Kim ◽  
Jeong Kuk Park ◽  
HyoJin Song ◽  
SangYoun Park
Keyword(s):  
Streptomyces Coelicolor ◽  
Crystallographic Analysis ◽  
Terminal Region ◽  
Full Length ◽  
Spectrometric Analysis ◽  
X Rays ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Parameters ◽  
Carboxyl Terminal

Full-length SigR fromStreptomyces coelicolorA3(2) was overexpressed inEscherichia coli, purified and submitted to crystallization trials using either polyethylene glycol 3350 or 4000 as a precipitant. X-ray diffraction data were collected to 2.60 Å resolution under cryoconditions using synchrotron X-rays. The crystal packs in space groupP43212, with unit-cell parametersa=b= 42.14,c= 102.02 Å. According to the Matthews coefficient, the crystal asymmetric unit cannot contain the full-length protein. Molecular replacement with the known structures of region 2 and region 4 as independent search models indicates that the crystal contains only the −35 element-binding carboxyl-terminal region 4 of full-length SigR. Mass-spectrometric analysis of the harvested crystal confirms this, suggesting a crystal volume per protein weight (VM) of 2.24 Å3 Da−1and 45.1% solvent content.

scholarly journals Cloning, expression, purification, crystallization and preliminary crystallographic analysis of 5-aminolaevulinic acid dehydratase fromBacillus subtilis

2010 ◽  
Vol 66 (9) ◽  
pp. 1053-1055 ◽  
Author(s):  
Qianda Lu ◽  
Jinming Ma ◽  
Hui Rong ◽  
Jun Fan ◽  
Ye Yuan ◽  
...  
Keyword(s):  
Crystallographic Analysis ◽  
Diffusion Method ◽  
X Ray Diffraction ◽  
Gene Encoding ◽  
Data Set ◽  
X Ray ◽  
Aminolaevulinic Acid ◽  
Acid Dehydratase ◽  
Strain Bl21 ◽  
Aminolaevulinic Acid Dehydratase

5-Aminolaevulinic acid dehydratase (ALAD), a crucial enzyme in the biosynthesis of tetrapyrrole, catalyses the condensation of two 5-aminolaevulinic acid (ALA) molecules to form porphobilinogen (PBG). The gene encoding ALAD was amplified from genomic DNA ofBacillus subtilisand the protein was overexpressed inEscherichia colistrain BL21 (DE3). The protein was purified and crystallized with an additional MGSSHHHHHHSSGLVPRGSH– tag at the N-terminus of the target protein. Diffraction-quality single crystals were obtained by the hanging-drop vapour-diffusion method. An X-ray diffraction data set was collected at a resolution of 2.7 Å.

scholarly journals Purification, crystallization and preliminary crystallographic analysis of a 4-thiouridine synthetase–RNA complex

2013 ◽  
Vol 69 (4) ◽  
pp. 421-424 ◽  
Author(s):  
Peter-Thomas Naumann ◽  
Charles T. Lauhon ◽  
Ralf Ficner
Keyword(s):  
Diffraction Data ◽  
Thermotoga Maritima ◽  
Crystallographic Analysis ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Orthorhombic Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Dependent Modification ◽  
Rna Complex

The sulfurtransferase 4-thiouridine synthetase (ThiI) is involved in the ATP-dependent modification of U8 in tRNA. ThiI fromThermotoga maritimawas cloned, overexpressed and purified. A complex comprising ThiI and a truncated tRNA was prepared and crystallized, and X-ray diffraction data were collected to a resolution of 3.5 Å. The crystals belonged to the orthorhombic space groupP212121, with unit-cell parametersa= 102.9,b= 112.8,c= 132.8 Å.

High-Intensity Rotating Anode X-Ray Tubes

1965 ◽  
Vol 9 ◽  
pp. 194-201
Author(s):  
A. Taylor
Keyword(s):  
Power Dissipation ◽  
Rotational Speed ◽  
High Intensity ◽  
High Pressures ◽  
Focal Spot ◽  
Spot Size ◽  
Focal Spot Size ◽  
X Ray

AbstractDemountable rotating anode X-ray tubes with a 7½ kW power dissipation have been built for conventional diffraction work with powder cameras and equi-inclination Weissenberg goniometers, and for use with a tetrahedral press for studying crystalline matter at ultra-high pressures. The tubes employ a highly compact cooling and sealing arrangement on the rotating anode which enables four windows to be used with the focal spot close to the specimen. A rotational speed of 1750 rpm with a focal spot size of 10 × 1 mm enables the tubes to be operated at 250–275 mA at 30 kV DC or at 150 mA, 50 kV DC.

Focal construct geometry for high-intensity x-ray diffraction from laser-shocked polycrystalline

2020 ◽  
Vol 91 (8) ◽  
pp. 083908
Author(s):  
XiaoHui Chen ◽  
Bo Li ◽  
Tao Xue ◽  
Jun Li
Keyword(s):  
High Intensity ◽  
X Ray Diffraction ◽  
X Ray

scholarly journals Expression, purification, crystallization and preliminary X-ray crystallographic analysis of Enpp6

2014 ◽  
Vol 70 (6) ◽  
pp. 794-799 ◽  
Author(s):  
Junko Morita ◽  
Kazuki Kato ◽  
Emiko Mihara ◽  
Ryuichiro Ishitani ◽  
Junichi Takagi ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Crystallographic Analysis ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Data Set ◽  
X Ray ◽  
Cell Parameters ◽  
Choline Metabolism ◽  
Protein Molecules ◽  
Membrane Bound

Enpp (ectonucleotide phosphodiesterase/pyrophosphatase) 6 is a membrane-bound glycoprotein that hydrolyzes choline-containing compounds such as lysophosphatidylcholine and glycerophosphorylcholine, and presumably participates in choline metabolism. The catalytic domain of mouse Enpp6 was expressed in HEK293T cells, purified using the TARGET tag/P20.1-Sepharose system and crystallized. An X-ray diffraction data set was collected to 1.8 Å resolution. The crystal belonged to space groupP1, with unit-cell parametersa= 63.7,b= 68.8,c= 69.7 Å, α = 60.6, β = 87.0, γ = 68.1°. Assuming the presence of two protein molecules per asymmetric unit, the solvent content was estimated to be 49.5%.

scholarly journals Purification, crystallization and X-ray crystallographic analysis of human RAB11(S20V), a constitutively active GTP-binding form

2015 ◽  
Vol 71 (10) ◽  
pp. 1247-1250 ◽  
Author(s):  
Chang Min Kim ◽  
Jae Young Choi ◽  
Jong Hwan Yoon ◽  
Hyun Ho Park
Keyword(s):  
Crystallographic Analysis ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Gtp Hydrolysis ◽  
X Ray ◽  
Cell Parameters ◽  
Gtp Binding ◽  
His Tag ◽  
Hydrolysis Activity ◽  
Constitutively Active

RAB11, a member of the Ras superfamily of small G proteins, is involved in the regulation of vesicle trafficking during endosome recycling. Substitution of Ser20 by Val20 in Rab11 [RAB11(S20V)] inhibits its GTP hydrolysis activity and produces a constitutively active GTP-binding form. In this study, the RAB11(S20V) mutant was overexpressed inEscherichia coliwith an engineered C-terminal His tag. RAB11(S20V) was then purified to homogeneity and was crystallized at 293 K. X-ray diffraction data were collected to a resolution of 2.4 Å from a crystal belonging to space groupI4, with unit-cell parametersa = 74.11,b= 74.11,c= 149.44 Å. The asymmetric unit was estimated to contain two molecules of RAB11(S20V).

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