scholarly journals Frq2 fromDrosophila melanogaster: cloning, expression, purification, crystallization and preliminary X-ray analysis

2014 ◽  
Vol 70 (4) ◽  
pp. 530-534 ◽  
Author(s):  
Soledad Baños-Mateos ◽  
Antonio Chaves-Sanjuán ◽  
Alicia Mansilla ◽  
Alberto Ferrús ◽  
María José Sánchez-Barrena
Keyword(s):  
Nervous System ◽  
Drosophila Melanogaster ◽  
Crystal Structures ◽  
Calcium Binding ◽  
Crystallographic Analysis ◽  
Differential Function ◽  
Crystal Forms ◽  
X Ray ◽  
Seeding Method ◽  
Chromatographic Procedure

Drosophila melanogastercontains two calcium-binding proteins, Frq1 and Frq2, in the nervous system that control the number of synapses and the probability of release. To understand the differential function of the two proteins, whose sequence is only 5% dissimilar, the crystal structures of Frq1 and Frq2 are needed. Here, the cloning, expression, purification, crystallization and preliminary crystallographic analysis of Frq2 are presented. The full-length protein was purified using a two-step chromatographic procedure. Two different diffracting crystal forms were obtained using a progressive streak-seeding method and detergents.

Imidazole/benzimidazole-modified cyclotriphosphazenes as highly selective fluorescent probes for Cu2+: synthesis, configurational isomers, and crystal structures

2017 ◽  
Vol 46 (28) ◽  
pp. 9140-9156 ◽  
Author(s):  
Aylin Uslu ◽  
Süreyya Oğuz Tümay ◽  
Ahmet Şenocak ◽  
Fatma Yuksel ◽  
Elif Özcan ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Fluorescent Probes ◽  
Copper Ion ◽  
Crystallographic Analysis ◽  
Ion Detection ◽  
X Ray

We present a comprehensive work and discuss the fluoroprobe properties of synthesized compounds for copper ion detection with a stereochemical approach using X-ray crystallographic analysis results.

scholarly journals Overexpression, crystallization and preliminary X-ray crystallographic analysis of the ectoine hydroxylase fromSphingopyxis alaskensis

2014 ◽  
Vol 70 (4) ◽  
pp. 493-496 ◽  
Author(s):  
Astrid Hoeppner ◽  
Nils Widderich ◽  
Erhard Bremer ◽  
Sander H. J. Smits
Keyword(s):  
Crystallographic Analysis ◽  
Diffusion Method ◽  
Oxidative Decarboxylation ◽  
Expression And Purification ◽  
Crystal Forms ◽  
X Ray ◽  
Mononuclear Iron ◽  
Vapour Diffusion ◽  
Purification Protocol

The ectoine hydroxylase (EctD) is a member of the non-haem-containing iron(II)- and 2-oxoglutarate-dependent dioxygenase superfamily. Its mononuclear iron centre is a prerequisite for the activity of this enzyme and promotes the O2-dependent oxidative decarboxylation of 2-oxoglutarate, which is coupled to a two-electron oxidation of the substrate ectoine to yield 5-hydroxyectoine. An expression and purification protocol for the EctD enzyme fromSphingopyxis alaskensiswas developed and the protein was crystallized using the sitting-drop vapour-diffusion method. This resulted in two different crystal forms, representing the apo and iron-bound forms of the enzyme.

Solvent–guest control of two extremely similar tetrahydrofuran inclusion structures

2014 ◽  
Vol 70 (1) ◽  
pp. 126-131 ◽  
Author(s):  
Jiabin Gao ◽  
Mohan M. Bhadbhade ◽  
Roger Bishop
Keyword(s):  
Crystal Structures ◽  
Inclusion Compounds ◽  
Crystal Form ◽  
Solvent Free ◽  
Guest Molecules ◽  
Crystal Forms ◽  
X Ray

Racemic 2,4,6,8-tetracarbomethoxybicyclo[3.3.0]octa-2,6-diene-3,7-diol, C16H18O10(1), was known previously to yield two solvent-free polymorphs and also a clathrate inclusion crystal form. Crystallization of (1) yields two inclusion compounds containing tetrahydrofuran (THF): (1)4·THF is obtained from a mixture of THF and methanol, whereas (1)2·THF is obtained from pure THF. The X-ray crystal structures reveal that the two compounds are extremely similar and that their host arrangements are essentially identical. They differ, however, in the proportion, orientation and host–guest interaction of the included THF molecules. The disordered guest molecules in (1)4·THF are oriented along the guest channel direction, whereas in (1)2·THF they lie across the channel. This unusual solvent–guest control of inclusion structures has implications relating to the formation of polymorphic structures and other competing crystal forms.

Intramolecular Hydrolysis of Coordinated Acetonitrile in a Binuclear Complex of Cobalt(III): X-Ray Crystallographic Analysis of Salts of [(tren)Co(μ-NH2,μ-L)Co(tren)]4+(L=OH, CH3C(O)NH)

1990 ◽  
Vol 43 (4) ◽  
pp. 643 ◽  
Author(s):  
NW Alcock ◽  
II Creaser ◽  
NJ Curtis ◽  
L Roecker ◽  
AM Sargeson ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Binuclear Complex ◽  
Binding Mode ◽  
Crystallographic Analysis ◽  
Bridging Ligands ◽  
X Ray ◽  
Hydrolysis Of

A synthesis of [( tren )Co(μ-NH2,μ-OH)Co( tren )]4+(3)( tren = tris (2- aminoethyl )amine) is reported along with a series of derivatives: [( tren ) XCo (μ-NH2) CoX ( tren )]n+, where X = CF3SO3- (n = 3)(4), X = CH3CN (n = 5)(5), and [( tren )Co(μ-NH2,μ-CH3C(O)NH)Co( tren )]4+ (6). The substitution of (4) by CH3CN to yield (5) was studied in CH3CN at 20°C, k = 9.0×10-3 s-1, and the intramolecular hydrolysis of (5) to yield the bridging acetamide complex (6) was studied at various acid concentrations. The X-ray crystal structures were determined for (3b) (exafluorophosphate, dihydrate) and (6b) (dithionate, tetrahydrate ). Both crystals are monoclinic, respectively P21/n with a 11.082(2), b 10.402(2), c 15.611(2)Ǻ, β 99.13(2)°, Z 2, and C2/c with a 14.328(2), b 14.046(1), c 16.497(2)Ǻ, β 101.90(1)°, Z 4. For the salt of (3), 2389 data with 1 ≥ 2σ(I) were refined to R 0.070 ( Rw 0.066), and, for the salt of (6), 3087 data with I ≥ 3σ(I) were refined to R 0.041 ( Rw 0.056). Both ions lie on pseudo-symmetric sites involving disorder of the bridging ligands . The structures establish the binding mode of the acetamido ion and the orientation of the tren groups in the isolated complexes.

Chemistry and crystal structures of tetrabenzoylethylene, its photolysis product and tetraacetylethylene

1978 ◽  
Vol 31 (6) ◽  
pp. 1265 ◽  
Author(s):  
JR Cannon ◽  
VA Patrick ◽  
CL Raston ◽  
AH White
Keyword(s):  
Solid State ◽  
Crystal Structures ◽  
Molecular Conformation ◽  
Crystallographic Analysis ◽  
Stable Form ◽  
Photolysis Product ◽  
Molecular Conformations ◽  
X Ray ◽  
The Difference ◽  
The Stability

X-ray crystallographic analysis has revealed that the light-sensitive form (A) and the light-stable form (A') of tetrabenzoylethylene are not valence tautomers but are two crystalline modifications of the same substance. The difference in the stability of these forms to light appears to be a consequence of their different molecular conformations and packing in the solid state. The molecular conformation of the A form is represented by (8) and that of the A' form by (9). The related tetraacetylethylene has the conformation (10) in the solid state. X-ray crystallographic analysis has also revealed that the photolysis product (B) of tetrabenzoylethylene is 4-phenoxy-3,4,6-triphenyl-1H,4H-furo[3,4-c]-furan-1-one (11). ��� The crystal structures of (8), (9), (10) and (11) were determined by X-ray diffraction: diffractometer data at 295 K were refined by least-squares techniques to residuals of 0.064 (2161 'observed' reflections) for (8), 0.057 (1310) for (9), 0.049 (1295) for (10) and 0.061 (1639) for (11). Crystals of (8) are monoclinic, P21/n, a 8.775(5), b 17.352(9), c 30.985(8)Ǻ, β 93.01(3)°, Z 8. Crystals of (9) which contain carbon disulfide are monoclinic, A2/a, a 21.21(2), b 6.181(4), c 20.35(2) Ǻ, β 102.77(7)°, Z 4. Crystals of (10) are monoclinic, P21/n, a 7.540(2), b 4.392(2), c 14.770(4) Ǻ, β 96.29(2)°, Z 2. Crystals of (11) are monoclinic, P1/n, a 14.820(4), b 15.000(3), c 10.819(4)Ǻ, β 106.02(2)°, Z 4.

Crystallization and X-ray crystallographic analysis of m-calpain, a Ca2+-dependent protease

1999 ◽  
Vol 55 (8) ◽  
pp. 1484-1486 ◽  
Author(s):  
Christopher M. Hosfield ◽  
Qilu Ye ◽  
J. Simon C. Arthur ◽  
Carol Hegadorn ◽  
Dorothy E. Croall ◽  
...  
Keyword(s):  
Proteolytic Activity ◽  
Cysteine Proteases ◽  
Crystallographic Analysis ◽  
Crystal Forms ◽  
X Ray ◽  
Anomalous Data ◽  
Absolute Requirement ◽  
The Absolute

The absolute requirement of Ca2+ for proteolytic activity is a feature unique to the calpains, a family of heterodimeric cysteine proteases. Conditions are described which give rise to diffraction-quality crystals of m-calpain in two crystal forms, P1 and P21. Data have been collected from native crystals of m-calpain in both P1 and P21 forms, to 2.6 and 2.15 Å, respectively. Selenomethionine-containing crystals have been grown in both forms, and anomalous data from the P21 selenomethionine enzyme provided the location of 17 of the 19 Se atoms in the protein.

Stereoselective synthesis and X-ray crystallographic analysis of mixed 6,6-dihalo penicillanates

1985 ◽  
Vol 63 (11) ◽  
pp. 3177-3181 ◽  
Author(s):  
Diego U. Belinzoni ◽  
Oreste A. Mascaretti ◽  
Pedro M. Alzari ◽  
Graciela Punte ◽  
Carlos Faerman ◽  
...  
Keyword(s):  
Single Crystal ◽  
Crystal Structures ◽  
Stereoselective Synthesis ◽  
Crystallographic Analysis ◽  
Displacement Reaction ◽  
X Ray ◽  
Single Crystal Analysis

The pivaloyloxy methyl 6,6-dihalo penicillanates 1a, 1b, and 1c have been stereoselectively prepared from the reaction of pivaloyloxy methyl 6-diazo penicillanate 2 with either N-halosuccinimide/halide or the interhalogens Xl (X = Cl, Br). The crystal structures of 3S,5R,6R pivaloyloxy methyl 6-bromo, 6-chloro penicillanate1a; 3S,5R,6R pivaloyloxy methyl 6-iodo, 6-bromo penicillanate 1b, and 3S, 5R, 6R pivaloyloxymethyl 6-iodo, 6-chloro penicillanate 1c have been determined by X-ray single crystal analysis. The stereochemistry of the displacement reaction is discussed.

What can Crystallographic Analysis tell us About Fibrinogen?

1979 ◽  
Author(s):  
Carolyn Cohen ◽  
John W. Weisel
Keyword(s):  
Electron Microscopy ◽  
Protein Molecule ◽  
Crystallographic Analysis ◽  
X Ray Diffraction ◽  
Technical Problems ◽  
Crystal Forms ◽  
X Ray ◽  
X Ray Crystallography ◽  
Large Size ◽  
Hydrated Protein

A major project in our laboratory has been the determination of the molecular structure of fibrinogen and its Interactions to form fibrin. We have approached this problem by attempting to obtain ordered forms of fibrinogen and, In fact, to crystallize the molecule. X-ray crystallography is the only objective method that can yield the detailed structure of the native hydrated protein molecule. In order to obtain crystals of fibrinogen, we found that limited proteolytic digestion is required. We have now produced three macroscopic crystal forms and a variety of microcrystals using several different enzymes and fibrinogens from different species. These modified molecules are largely intact and retain their biological function to form clots with thrombin similar in appearance to native fibrin by electron microscopy. The degree of order in all these aggregates is, moreover, far superior to that of fibrin. Some of the microcrystalline forms have been shown to be closely related to fibrin. Since the fibrinogen molecule is several times larger than any protein yet solved by X-ray methods, the technical problems in the crystallographic analysis are formidable. Because of the large size of the molecule, however, electron microscopy provides Information essential for the solution. We have completed a preliminary X-ray characterization of the ctystals and, using coordinated X-ray diffraction and electron microscopy, deduced plausible packing models. The results from this first stage in the X-ray analysis of fibrinogen give insight also into the packing of the molecules to form fibrin. Supported by USPHS grant #AM17346.

scholarly journals Syntheses and Crystal Structures of and

2010 ◽  
Vol 2010 ◽  
pp. 1-6 ◽  
Author(s):  
Takayoshi Fujii ◽  
Mihoko Kanno ◽  
Mitsuo Hirata
Keyword(s):  
Crystal Structures ◽  
Crystallographic Analysis ◽  
Planar Geometry ◽  
Distorted Tetrahedron ◽  
X Ray ◽  
Trinuclear Complexes ◽  
Square Planar

We have prepared the trinuclear complexes (3) and (4), from the reaction of with (1) and determined their structures by X-ray crystallographic analysis. In both complexes, two monoanions chelate the Cu(II) center in square-planar geometry, whereas the terminal Cu(II) center is four-coordinate and a distorted tetrahedron.

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