scholarly journals Crystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region

2010 ◽  
Vol 66 (9) ◽  
pp. 1071-1073 ◽  
Author(s):  
Cerrone Cabanos ◽  
Hiroyuki Urabe ◽  
Taro Masuda ◽  
Mary Rose Tandang-Silvas ◽  
Shigeru Utsumi ◽  
...  
Keyword(s):  
Sodium Citrate ◽  
Three Dimensional ◽  
Core Region ◽  
Dimensional Structure ◽  
Monoclinic Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Peg 400 ◽  
Ara H 1 ◽  
Peanut Allergens

Peanuts contain some of the most potent food allergens known to date. Ara h 1 is one of the three major peanut allergens. As a first step towards three-dimensional structure elucidation, recombinant Ara h 1 core region was cloned, expressed inEscherichia coliand purified to homogeneity. Crystals were obtained using 0.1 Msodium citrate pH 5.6, 0.1 MNaCl, 15% PEG 400 as precipitant. The crystals diffracted to 2.25 Å resolution using synchrotron radiation and belonged to the monoclinic space groupC2, with unit-cell parametersa= 156.521,b= 88.991,c= 158.971 Å, β = 107.144°. Data were collected at the BL-38B1 station of SPring-8 (Hyogo, Japan).

scholarly journals Crystallization and preliminary X-ray diffraction analysis of a single variable domain of the immunoglobulin superfamily in amphioxus,Amphi-IgSF-V

2014 ◽  
Vol 70 (8) ◽  
pp. 1072-1075 ◽  
Author(s):  
Bo Jiang ◽  
Yanjie Liu ◽  
Rong Chen ◽  
Zhenbao Wang ◽  
Mansoor Tariq ◽  
...  
Keyword(s):  
Immune System ◽  
Structural Information ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Immunoglobulin Superfamily ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Parameters ◽  
System A ◽  
Human Immunoglobulins

Amphioxus is regarded as an essential animal model for the study of immune evolution. Discovery of new molecules with the immunoglobulin superfamily (IgSF) variable (V) domain in amphioxus would help in studying the evolution of IgSF V molecules in the immune system. A protein was found which just contains only one IgSF V domain in amphioxus, termedAmphi-IgSF-V; it has over 30% sequence identity to the V domains of human immunoglobulins and mammalian T-cell receptors. In order to clarify the three-dimensional structure of this new molecule in amphioxus,Amphi-IgSF-V was expressed, purified and crystallized, and diffraction data were collected to a resolution of 1.95 Å. The crystal belonged to space groupP3221, with unit-cell parametersa=b= 53.9,c= 135.5 Å. The Matthews coefficient and solvent content were calculated to be 2.58 Å3 Da−1and 52.38%, respectively. The results will provide structural information to study the evolution of IgSF V molecules in the immune system.

scholarly journals Crystallization and preliminary X-ray diffraction studies of the family 54 carbohydrate-binding module from laminarinase (β-1,3-glucanase) Lic16A ofClostridium thermocellum

2015 ◽  
Vol 71 (2) ◽  
pp. 217-220 ◽  
Author(s):  
Yury A. Kislitsyn ◽  
Valeriya R. Samygina ◽  
Igor A. Dvortsov ◽  
Nataliya A. Lunina ◽  
Inna P. Kuranova ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Dimensional Structure ◽  
Diffusion Method ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Parameters ◽  
The Family ◽  
Overexpression System

The crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding module (CBM) from laminarinase Lic16A of the hyperthermophilic anaerobic bacteriumClostridium thermocellum(ctCBM54) are reported. Recombinant ctCBM54 was prepared using anEscherichia coli/pQE30 overexpression system and was crystallized by the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 2.1 Å resolution using synchrotron radiation. The crystals belonged to space groupP6322, with unit-cell parametersa=b= 130.15,c= 131.05 Å. The three-dimensional structure of ctCBM54 will provide valuable information about the structure–function relation of the laminarinase Lic16A and will allow the exploitation of this binding module in biotechnological applications.

scholarly journals Purification, crystallization and preliminary X-ray diffraction analysis of theEscherichia colicommon pilus chaperone EcpB

2015 ◽  
Vol 71 (6) ◽  
pp. 676-679 ◽  
Author(s):  
James A. Garnett ◽  
Mamou Diallo ◽  
Steve J. Matthews
Keyword(s):  
Heavy Atom ◽  
Three Dimensional ◽  
Solid Surfaces ◽  
Dimensional Structure ◽  
Molecular Replacement ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Parameters ◽  
The Common ◽  
First Time

Pili are key cell-surface components that allow the attachment of bacteria to both biological and abiotic solid surfaces, whilst also mediating interactions between themselves. InEscherichia coli, the common pilus (Ecp) belongs to an alternative chaperone–usher (CU) pathway that plays a major role in both early biofilm formation and host-cell adhesion. The chaperone EcpB is involved in the biogenesis of the filament, which is composed of EcpA and EcpD. Initial attempts at crystallizing EcpB using natively purified protein from the bacterial periplasm were not successful; however, after the isolation of EcpB under denaturing conditions and subsequent refolding, crystals were obtained at pH 8.0 using the sitting-drop method of vapour diffusion. Diffraction data have been processed to 2.4 Å resolution. These crystals belonged to the trigonal space groupP3121 orP3221, with unit-cell parametersa=b= 62.65,c= 121.14 Å and one monomer in the asymmetric unit. Molecular replacement was unsuccessful, but selenomethionine-substituted protein and heavy-atom derivatives are being prepared for phasing. The three-dimensional structure of EcpB will provide invaluable information on the subtle mechanistic differences in biogenesis between the alternative and classical CU pathways. Furthermore, this is the first time that this refolding strategy has been used to purify CU chaperones, and it could be implemented in similar systems where it has not been possible to obtain highly ordered crystals.

Crystal structure of lanthanum oxyorthosilicate, La2SiO5

2006 ◽  
Vol 21 (4) ◽  
pp. 300-303 ◽  
Author(s):  
Koichiro Fukuda ◽  
Tomoyuki Iwata ◽  
Eric Champion
Keyword(s):  
Crystal Structure ◽  
Structural Model ◽  
Rietveld Method ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Monoclinic Space Group ◽  
X Ray ◽  
Reliability Indices ◽  
Volumetric Expansion ◽  
Tricapped Trigonal Prism

The crystal structure of La2SiO5 was refined from laboratory X-ray powder diffraction data (CuKα1) using the Rietveld method. The crystal structure is monoclinic (space group P21∕c,Z=4) with lattice dimensions a=0.93320(2) nm, b=0.75088(1) nm, c=0.70332(1) nm, β=108.679(1)°, and V=0.46687(1) nm3. The final reliability indices were Rwp=7.14%, RP=5.52%, and RB=3.83%. There are two La sites in the structural model, La1 and La2. La1 is ninefold coordinated to oxygen, forming a tricapped trigonal prism with a mean La1-O distance of 0.263 nm. The La2O7 coordination polyhedron is a distorted capped octahedron with a mean La2-O distance of 0.251 nm. The La1O9 polyhedra share faces and the La2O7 polyhedra share edges, forming two sets of sheets that alternate parallel to the (100) plane. These sheets are linked through SiO4 tetrahedra and non-silicon-bonded oxygen atoms to form a three-dimensional structure. This compound is isomorphous with the low-temperature (X1) phases of R2SiO5 (R=Y and Gd). The volumes of RO9 polyhedra steadily increase with increasing ionic radius of R, from Y3+ to Gd3+ to La3+, which causes substantial volumetric expansion of the crystals.

scholarly journals Crystallization and preliminary X-ray diffraction studies of La1 fromLiocheles australasiae

2014 ◽  
Vol 70 (7) ◽  
pp. 915-917 ◽  
Author(s):  
Saori Kamachi ◽  
Junya Nagao ◽  
Masahiro Miyashita ◽  
Yoshiaki Nakagawa ◽  
Hisashi Miyagawa ◽  
...  
Keyword(s):  
Biological Function ◽  
Three Dimensional ◽  
Scorpion Venom ◽  
Dimensional Structure ◽  
Diffusion Method ◽  
Monoclinic Space Group ◽  
X Ray Diffraction ◽  
Cell Parameters ◽  
Factor Type ◽  
Von Willebrand

A novel scorpion venom peptide, La1 fromLiocheles australasiae, with a molecular weight of 7.8 kDa, is presumed to possess a single von Willebrand factor type C (VWC) domain, a common protein module, based on the position of eight Cys residues in its sequence. The biological function of La1 is still unknown. Deciphering its three-dimensional structure will be helpful in understanding its biological function. La1 was crystallized by the sitting-drop vapour-diffusion method using magnesium sulfate as a precipitant. The crystals belonged to the monoclinic space groupC2, with unit-cell parametersa= 63.0,b= 30.2,c= 32.3 Å, β = 108.5°, and diffracted to 1.9 Å resolution. The calculatedVMbased on one molecule per asymmetric unit was 1.87 Å3 Da−1. The solvent content was 34.1%.

scholarly journals Cloning, purification, crystallization and preliminary X-ray diffraction crystallographic study of acyl-protein thioesterase 1 fromSaccharomyces cerevisiae

2012 ◽  
Vol 68 (7) ◽  
pp. 775-777
Author(s):  
Ye Yuan ◽  
Xiao Wang ◽  
Xu Li ◽  
Maikun Teng ◽  
Liwen Niu ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Modification ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Crystallographic Study ◽  
Preliminary Model

Palmitoylation/depalmitoylation plays an important role in protein modification. yApt1 is the only enzyme inSaccharomyces cerevisiaethat catalyses depalmitoylation. In the present study, recombinant full-length yApt1 was cloned, expressed, purified and crystallized. The crystals diffracted to 2.40 Å resolution and belonged to space groupP42212, with unit-cell parametersa = b = 146.43,c = 93.29 Å. A preliminary model of the three-dimensional structure has been built and further refinement is ongoing.

scholarly journals Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato

1999 ◽  
Vol 55 (12) ◽  
pp. 2051-2052 ◽  
Author(s):  
Gerhard Schenk ◽  
Lyle E. Carrington ◽  
Susan E. Hamilton ◽  
John de Jersey ◽  
Luke W. Guddat
Keyword(s):  
Acid Phosphatase ◽  
Sweet Potato ◽  
Diffraction Data ◽  
Three Dimensional ◽  
Purple Acid Phosphatase ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Parameters ◽  
The Subject

Purple acid phosphatase from sweet potato is a homodimer of 110 kDa. Two forms of the enzyme have been characterized. One contains an Fe–Zn centre similar to that previously reported for red kidney bean purple acid phosphatase. Another isoform, the subject of this work, is the first confirmed example of an Fe–Mn-containing enzyme. Crystals of this protein have been grown from PEG 6000. They have unit-cell parameters a = b = 118.4, c = 287.4 Å and have the symmetry of space group P6522, with one dimer per asymmetric unit. Diffraction data collected using a conventional X-ray source from a cryocooled crystal extend to 2.90 Å resolution. The three-dimensional structure of the enzyme will provide insight into the coordination of this novel binuclear metal centre.

scholarly journals Crystallization and preliminary X-ray diffraction studies of mammalian purple acid phosphatase

1999 ◽  
Vol 55 (8) ◽  
pp. 1462-1464 ◽  
Author(s):  
Luke W. Guddat ◽  
Alan S. McAlpine ◽  
David Hume ◽  
John de Jersey ◽  
Susan Hamilton ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Rational Design ◽  
Three Dimensional ◽  
Allantoic Fluid ◽  
Bone Diseases ◽  
Purple Acid Phosphatase ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Parameters

The oxidized form of purple acid phosphatase from pig allantoic fluid has been crystallized in the presence of phosphate using the hanging-drop technique. The crystals belong to the space group P212121 and have unit-cell parameters a = 66.8, b = 70.3, c = 78.7 Å. Diffraction data collected from a cryocooled crystal using a conventional X-ray source extend to 1.55 Å resolution. A knowledge of the three-dimensional structure of mammalian purple acid phosphatase will aid in understanding the substrate specificity of the enzyme and will be important in the rational design of inhibitors, with potential in the treatment of bone diseases.

scholarly journals Purification, crystallization and characterization of thePseudomonasouter membrane protein FapF, a functional amyloid transporter

2016 ◽  
Vol 72 (12) ◽  
pp. 892-896 ◽  
Author(s):  
Sarah L. Rouse ◽  
Wlliam J. Hawthorne ◽  
Sebastian Lambert ◽  
Marc L. Morgan ◽  
Stephen A. Hare ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Limited Proteolysis ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Monoclinic Space Group ◽  
The Novel ◽  
Functional Amyloid ◽  
Cell Parameters ◽  
Bacterial Outer Membrane

Bacteria often produce extracellular amyloid fibresviaa multi-component secretion system. Aggregation-prone, unstructured subunits cross the periplasm and are secreted through the outer membrane, after which they self-assemble. Here, significant progress is presented towards solving the high-resolution crystal structure of the novel amyloid transporter FapF fromPseudomonas, which facilitates the secretion of the amyloid-forming polypeptide FapC across the bacterial outer membrane. This represents the first step towards obtaining structural insight into the products of thePseudomonasfapoperon. Initial attempts at crystallizing full-length and N-terminally truncated constructs by refolding techniques were not successful; however, after preparing FapF106–430from the membrane fraction, reproducible crystals were obtained using the sitting-drop method of vapour diffusion. Diffraction data have been processed to 2.5 Å resolution. These crystals belonged to the monoclinic space groupC121, with unit-cell parametersa= 143.4,b= 124.6,c= 80.4 Å, α = γ = 90, β = 96.32° and three monomers in the asymmetric unit. It was found that the switch to complete detergent exchange into C8E4 was crucial for forming well diffracting crystals, and it is suggested that this combined with limited proteolysis is a potentially useful protocol for membrane β-barrel protein crystallography. The three-dimensional structure of FapF will provide invaluable information on the mechanistic differences of biogenesis between the curli and Fap functional amyloid systems.

scholarly journals The crystal structure and spectroscopic properties of catena- (2-methylimidazolium bis(μ2-chloro)-aqua-chloromanganese(II))

2011 ◽  
Vol 76 (2) ◽  
pp. 235-247 ◽  
Author(s):  
Barbara Hachuła ◽  
Monika Pędras ◽  
Maria Nowak ◽  
Joachim Kusz ◽  
Danuta Pentak ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Layer Structure ◽  
Three Dimensional ◽  
Spectroscopic Properties ◽  
Chloride Anion ◽  
Monoclinic Space Group ◽  
Stacking Interactions ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Parameters

? novel manganese(II) coordination polymer, catena-(2- methylimidazolium bis(?2-chloro)-aqua-chloromanganese(II)), {(C4H7N2)[MnCl3(H2O)]}n, was synthesized, structurally characterized by FTIR spectroscopy and confirmed by single crystal X-ray diffraction analysis. Thermogravimetric analysis and EPR spectroscopy of the compound were also performed. The colourless crystals of the complex were monoclinic, space group P21/c, with the cell parameters a = 11.298(2) ?, b = 7.2485(14) ?, c = 14.709(5) ?, ? = 128.861(18)?, V = 938.0(5) ?3, Z = 4 and R1 = 0.03. The title compound consisted of onedimensional infinite anionic chains [MnCl3(H2O)]n and isolated 2- methylimidazolium cations. The Mn(II) atom was octahedrally coordinated to four bridging chloride anions [Mn-Cl = 2.5109(6) - 2.5688(7) ?], one terminal chloride anion [Mn-Cl = 2.5068(11) ?] and a H2O molecule [Mn-O = 2.2351(17) ?]. A three-dimensional layer structure was constructed via hydrogen bonds and by weak ?-? stacking interactions. A four-step thermal decomposition occurred in the temperature range 25-900?C under nitrogen.

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