Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli

1999 ◽  
Vol 55 (6) ◽  
pp. 1226-1228 ◽  
Author(s):  
Tina Izard ◽  
Arie Geerlof ◽  
Ann Lewendon ◽  
John J. Barker
Keyword(s):  
Escherichia Coli ◽  
Packing Density ◽  
Coenzyme A ◽  
Unit Cell Dimension ◽  
Unit Cell ◽  
Cell Dimension ◽  
Asymmetric Unit ◽  
Cubic Crystals ◽  
Space Group ◽  
Better Than

Phosphopantetheine adenylyltransferase (PPAT, E.C. 2.7.7.3) catalyzes the penultimate step in coenzyme A (CoA) biosynthesis, transferring an adenylyl group from ATP to 4′-phosphopantetheine, and forming dephospho-CoA. Cubic crystals of native PPAT from Escherichia coli as well as PPAT in complex with its substrates were obtained. The crystals belong to space group I23 or I213 with unit-cell dimension a = 135.5 Å. The crystals diffract to better than 1.8 Å resolution on a Cu Kα rotating-anode generator. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 2.9 Å3 Da−1.

Rhombohedral crystals of 2-dehydro-3-deoxygalactarate aldolase from Escherichia coli

1999 ◽  
Vol 55 (7) ◽  
pp. 1368-1369 ◽  
Author(s):  
Nicholas C. Blackwell ◽  
Paul M. Cullis ◽  
Ronald A. Cooper ◽  
Tina Izard
Keyword(s):  
Escherichia Coli ◽  
Packing Density ◽  
Unit Cell ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters ◽  
K 12

2-Dehydro-3-deoxygalactarate (DDG) aldolase (E.C. 4.1.2.20) catalyzes the reversible aldol cleavage of DDG and 2-dehydro-3-deoxyglucarate to pyruvate and tartronic semialdehyde. Rhombohedral crystals of recombinant DDG aldolase from Escherichia coli K-12 were obtained. The crystals belong to space group R32 with unit-cell parameters a = 93 Å, α = 85°. The crystals diffract to beyond 1.8 Å resolution on a Cu Kα rotating-anode generator. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 1.34 Å3 Da−1.

scholarly journals N-Acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms

1999 ◽  
Vol 55 (7) ◽  
pp. 1350-1352 ◽  
Author(s):  
Fernando Gil ◽  
Santiago Ramón-Maiques ◽  
Alberto Marina ◽  
Ignacio Fita ◽  
Vicente Rubio
Keyword(s):  
Escherichia Coli ◽  
Specific Activity ◽  
High Specific Activity ◽  
Unit Cell ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters ◽  
E Coli ◽  
Carbamate Kinase

The gene for Escherichia coli N-acetyl-L-glutamate kinase (NAGK) was cloned in a plasmid and expressed in E. coli, allowing enzyme purification in three steps. NAGK exhibits high specific activity (1.1 µmol s−1 mg−1), lacks Met1 and forms dimers (shown by cross-linking). Crystals of unliganded NAGK diffract to 2 Å and belong to space group P6122 or its enantiomorph P6522 (unit-cell parameters a = b = 78.6, c = 278.0 Å) with two monomers in the asymmetric unit. Crystals of NAGK with acetylglutamate and the ATP analogue AMPPNP diffract to 1.8 Å and belong to space group C2221 (unit-cell parameters a = 60.0, b = 71.9, c = 107.4 Å), with one monomer in the asymmetric unit. NAGK crystallization will allow the determination of proposed structural similarities to carbamate kinase.

Crystallization of the N-terminal domain of the Escherichia coli regulatory protein TyrR

1999 ◽  
Vol 55 (11) ◽  
pp. 1923-1924 ◽  
Author(s):  
Kirsty H. R. MacPherson ◽  
Paul D. Carr ◽  
Denis Verger ◽  
Terry Kwok ◽  
Barrie E. Davidson ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Regulatory Protein ◽  
Unit Cell ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters ◽  
Terminal Domain

The N-terminal domain of the regulatory protein TyrR from Escherichia coli forms a dimer in solution and has been purified and crystallized. The crystals belong to space group C2 with unit-cell parameters a = 134.5, b = 72.1, c = 96.7 Å, β = 98.5°. The crystals diffract to 2.8 Å. Assuming a molecular weight of 23219 Da, a Vm of 2.5 Å3 Da−1 is obtained for two dimers in the asymmetric unit.

An X-ray examination of mordenite (ptilolite)

1938 ◽  
Vol 25 (163) ◽  
pp. 212-216 ◽  
Author(s):  
C. Waymouth ◽  
P. C. Thornely ◽  
W. H. Taylor
Keyword(s):  
Experimental Data ◽  
Unit Cell Dimension ◽  
Unit Cell ◽  
Cell Dimension ◽  
Complete Analysis ◽  
Private Communication ◽  
Space Group ◽  
X Ray ◽  
Ray Methods ◽  
Fibrous Zeolites

The structures of the fibrous zeolites edingtonite, thomsonite, and natrolite (with scolecite and mesolite) were determined by X-ray methods some years ago, and it was suggested shortly afterwards by M. H. Hey and F. A. Bannister in a private communication to one of us (W.H.T.) that ‘ptilolite’, another zeolite of fibrous habit, might prove to have a similar structure. An X-ray rotation photograph about the needle axis indicated a unit-cell dimension along the needle axis of approximately 7·5 Å., quite different from the axis c 6·6 Å. characteristic of the fibrous zeolites previously examined, and no further examination of ‘ptilolite’ was made at that time. We have now determined the unit cell and space-group of this crystal, and further work is in progress with a view to the complete analysis of the structure. This paper presents an account of the experimental data which we have obtained.

scholarly journals Crystallization and X-ray diffraction analysis of native and selenomethionine-substituted PhyH-DI fromBacillussp. HJB17

2017 ◽  
Vol 73 (11) ◽  
pp. 607-611
Author(s):  
Fang Lu ◽  
Bei Zhang ◽  
Yong Liu ◽  
Ying Song ◽  
Gangxing Guo ◽  
...  
Keyword(s):  
Unit Cell ◽  
Diffusion Method ◽  
Data Sets ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Solvent Content ◽  
Space Group ◽  
X Ray ◽  
Cell Parameters

Phytases are phosphatases that hydrolyze phytates to less phosphorylatedmyo-inositol derivatives and inorganic phosphate. β-Propeller phytases, which are very diverse phytases with improved thermostability that are active at neutral and alkaline pH and have absolute substrate specificity, are ideal substitutes for other commercial phytases. PhyH-DI, a β-propeller phytase fromBacillussp. HJB17, was found to act synergistically with other single-domain phytases and can increase their efficiency in the hydrolysis of phytate. Crystals of native and selenomethionine-substituted PhyH-DI were obtained using the vapour-diffusion method in a condition consisting of 0.2 Msodium chloride, 0.1 MTris pH 8.5, 25%(w/v) PEG 3350 at 289 K. X-ray diffraction data were collected to 3.00 and 2.70 Å resolution, respectively, at 100 K. Native PhyH-DI crystals belonged to space groupC121, with unit-cell parametersa = 156.84,b = 45.54,c = 97.64 Å, α = 90.00, β = 125.86, γ = 90.00°. The asymmetric unit contained two molecules of PhyH-DI, with a corresponding Matthews coefficient of 2.17 Å3 Da−1and a solvent content of 43.26%. Crystals of selenomethionine-substituted PhyH-DI belonged to space groupC2221, with unit-cell parametersa = 94.71,b= 97.03,c= 69.16 Å, α = β = γ = 90.00°. The asymmetric unit contained one molecule of the protein, with a corresponding Matthews coefficient of 2.44 Å3 Da−1and a solvent content of 49.64%. Initial phases for PhyH-DI were obtained from SeMet SAD data sets. These data will be useful for further studies of the structure–function relationship of PhyH-DI.

scholarly journals Crystallization and preliminary X-ray analysis of human rhinovirus serotype 2 (HRV2)

1999 ◽  
Vol 55 (8) ◽  
pp. 1459-1461 ◽  
Author(s):  
Núria Verdaguer ◽  
Thomas C. Marlovits ◽  
Jerónimo Bravo ◽  
David I. Stuart ◽  
Dieter Blaas ◽  
...  
Keyword(s):  
Potassium Phosphate ◽  
Attachment Site ◽  
Unit Cell ◽  
Human Rhinovirus ◽  
Intercellular Adhesion Molecule ◽  
Upper Respiratory Tract ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Cell Parameters

Human rhinoviruses, the major cause of mild recurrent infections of the upper respiratory tract, are small icosahedral particles. Over 100 different serotypes have been identified. The majority (91 serotypes) use intercellular adhesion molecule 1 as the cell-attachment site; ten serotypes (the minor group) bind to members of the low-density lipoprotein receptor. Three different crystal forms of the minor-group human rhinovirus serotype 2 (HRV2) were obtained by the hanging-drop vapour-diffusion technique using ammonium sulfate and sodium/potassium phosphate as precipitants. Monoclinic crystals, space group P21, diffracted at least to 2.8 Å resolution, and two complete virus particles were located in the crystal asymmetric unit. A second type of crystals had a compact cubic like morphology and diffracted beyond 2.5 Å resolution. These crystals belong to a primitive orthorhombic space group, with unit-cell parameters a = 309.3, b = 353.5, c = 759.6 Å, and contain one virus particle in the asymmetric unit. A third type of crystals, with a prismatic shape and belonging to space group I222, was also obtained under similar crystallization conditions. These latter crystals, with unit-cell parameters a = 308.7, b = 352.2, c = 380.5 Å, diffracted to high resolution (beyond 1.8 Å) and contained 15 protomers per asymmetric unit; this requires that three perpendicular crystal twofold axes coincide with three of the viral particle's dyad axes.

Structure of ζ-phase plutonium–uranium

1996 ◽  
Vol 52 (1) ◽  
pp. 32-37 ◽  
Author(s):  
A. C. Lawson ◽  
J. A. Goldstone ◽  
B. Cort ◽  
R. J. Martinez ◽  
F. A. Vigil ◽  
...  
Keyword(s):  
Thermal Expansion ◽  
Powder Diffraction ◽  
General Pattern ◽  
Neutron Powder Diffraction ◽  
Unit Cell ◽  
Asymmetric Unit ◽  
Space Group ◽  
Elastic Data ◽  
Primitive Unit Cell

The structure of the ζ-phase in the Pu—U system has been determined by neutron powder diffraction. The phase crystallizes in space group R{\bar 3}m with 58 atoms in the primitive unit cell and 10 atoms in the asymmetric unit. The structure is characterized by many short bonds and fits the general pattern of the light actinides. Thermal expansion and elastic data were obtained from the diffraction experiments.

scholarly journals Crystals of the Arp2/3 complex in two new space groups with structural information about actin-related protein 2 and potential WASP binding sites

2015 ◽  
Vol 71 (9) ◽  
pp. 1161-1168 ◽  
Author(s):  
Christopher T. Jurgenson ◽  
Thomas D. Pollard
Keyword(s):  
Binding Site ◽  
Structural Information ◽  
Unit Cell ◽  
Molecular Structures ◽  
Asymmetric Unit ◽  
Unit Cell Parameters ◽  
Space Group ◽  
Space Groups ◽  
Cell Parameters ◽  
New Space

Co-crystals of the bovine Arp2/3 complex with the CA motif from N-WASP in two new space groups were analyzed by X-ray diffraction. The crystals in the orthorhombic space groupP212121contained one complex per asymmetric unit, with unit-cell parametersa= 105.48,b= 156.71,c= 177.84 Å, and diffracted to 3.9 Å resolution. The crystals in the tetragonal space groupP41contained two complexes per asymmetric unit, with unit-cell parametersa=b= 149.93,c = 265.91 Å, and diffracted to 5.0 Å resolution. The electron-density maps of both new crystal forms had densities for small segments of subdomains 1 and 2 of Arp2. Both maps had density at the binding site on Arp3 for the C-terminal EWE tripeptide from N-WASP and a binding site proposed for the C motif of N-WASP in the barbed-end groove of Arp2. The map from the tetragonal crystal form had density near the barbed end of Arp3 that may correspond to the C helix of N-WASP. The noise levels and the low resolution of the maps made the assignment of specific molecular structures for any of these CA peptides impossible.

scholarly journals Crystal structure of gluconate 5-dehydrogenase from Lentibacter algarum

2020 ◽  
Vol 76 (5) ◽  
pp. 228-234
Author(s):  
Dengke Tian ◽  
Xueqi Fu ◽  
Wenqiang Cao ◽  
Hong Yuan
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Structural Similarity ◽  
Unit Cell ◽  
Unit Cell Parameters ◽  
Monoclinic System ◽  
Space Group ◽  
Cell Parameters ◽  
High Structural Similarity

Gluconate 5-dehydrogenase (Ga5DH; EC 1.1.1.69) from Lentibacter algarum (LaGa5DH) was recombinantly expressed in Escherichia coli and purified to homogeneity. The protein was crystallized and the crystal structure was solved at 2.1 Å resolution. The crystal belonged to the monoclinic system, with space group P1 and unit-cell parameters a = 55.42, b = 55.48, c = 79.16 Å, α = 100.51, β = 105.66, γ = 97.99°. The structure revealed LaGaDH to be a tetramer, with each subunit consisting of six α-helices and three antiparallel β-hairpins. LaGa5DH has high structural similarity to other Ga5DH proteins, demonstrating that this enzyme is highly conserved.

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