The structure determination of rabbit phosphoglucomutase

1981 ◽  
Vol 293 (1063) ◽  
pp. 205-208 ◽  
Keyword(s):  
Heavy Atom ◽  
Partial Solution ◽  
Relative Molecular Mass ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
X Ray ◽  
Tetragonal Crystals ◽  
Glycol Solution ◽  
Rotation Function

Tetragonal crystals of rabbit phosphoglucomutase have been grown from solutions containing ammonium sulphate, polyethylene glycol solution and enzyme. There are two molecules, each of relative molecular mass 64 000 per asymmetric unit. A rotation function suggests that these are related by a twofold axis. X-ray diffraction data for five heavy-atom derivatives and native crystals have been collected by using oscillation photography. A tentative and partial solution of the KAu(CN) 2 sites has been obtained. The enzyme in the native crystals is phosphorylated, but the phosphate can be removed without harm to the crystals. Similarly the essential Mg 2+ ion can be removed or replaced by Zn 2+ . The enzyme is active in the native crystals.

Crystallization and preliminary X-ray diffraction analysis of restriction endonuclease EcoRII

1999 ◽  
Vol 55 (9) ◽  
pp. 1604-1605 ◽  
Author(s):  
Elisavetta A. Karpova ◽  
Edward Meehan ◽  
Marc L. Pusey ◽  
Liqing Chen
Keyword(s):  
Restriction Endonuclease ◽  
Ammonium Sulfate ◽  
Function Analysis ◽  
Heavy Atom ◽  
Imaging Plate ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cell Parameters ◽  
Diffusion Technique ◽  
Rotation Function

Crystals of the restriction endonuclease EcoRII have been obtained by the vapor-diffusion technique in the presence of ammonium sulfate or polyethylene glycol. The best crystals were grown with ammonium sulfate as a precipitant. Crystals with dimensions of up to 0.6 × 0.6 × 0.6 mm have been observed. The crystals diffract to about 4.0 Å resolution at a cryo-temperature of 100 K using a rotating-anode X-ray source and a Rigaku R-AXIS IV imaging-plate detector. The space group has been determined to be either I23 or I213, with unit-cell parameters a = b = c = 160.3 Å, α = β = γ = 90°. The crystal asymmetric unit contains two protein molecules, and self-rotation function analysis shows a pseudo-twofold symmetry relating the two monomers. Attempts to improve the resolution of crystal diffraction and to search for heavy-atom derivatives are under way.

scholarly journals Crystallographic analysis of RsmA, a ribosomal RNA small subunit methyltransferase A fromStaphylococcus aureus

2015 ◽  
Vol 71 (8) ◽  
pp. 1063-1066 ◽  
Author(s):  
Yang Liu ◽  
Yuwei Zhu ◽  
Maikun Teng ◽  
Xu Li
Keyword(s):  
Staphylococcus Aureus ◽  
Ribosomal Rna ◽  
Small Subunit ◽  
Crystallographic Analysis ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Rotation Function

RsmA, a ribosomal RNA small subunit methyltransferase fromStaphylococcus aureus, catalyzes theN6methylation of adenine in 16S rRNA. In this study, RsmA fromStaphylococcus aureuswas cloned, expressed, purified and crystallized. The crystal belonged to space groupC2, with unit-cell parametersa= 84.38,b= 157.76,c= 96.50 Å, β = 95.04°. X-ray diffraction data were collected to a resolution of 3.2 Å. The self-rotation function and the Matthews coefficient suggested the presence of two molecules in the asymmetric unit.

Crystallization and preliminary X-ray diffraction of Trypanosoma cruzi dUTPase

1999 ◽  
Vol 55 (2) ◽  
pp. 528-530 ◽  
Author(s):  
V. Bernier-Villamor ◽  
A. Camacho ◽  
D. González-Pacanowska ◽  
E. Cedergren-Zeppezauer ◽  
A. Antson ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Unit Cell ◽  
The Self ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Solvent Content ◽  
X Ray ◽  
Cell Dimensions ◽  
Unit Cell Dimensions ◽  
Rotation Function

Crystals of Trypanosoma cruzi dUTPase have been grown. Two different morphologies are observed, depending on the molecular weight of the PEG used as precipitating agent in the mother liquor, both having a hexagonal unit cell with similar dimensions. Complete X-ray diffraction data have been collected to low resolution for one of the forms. The space group is P6322, with unit-cell dimensions a = 134.15, c = 147.05 Å. Peaks in the self-rotation function and the solvent content are consistent with two molecules of dUTPase per asymmetric unit.

scholarly journals Schaurteite, Ca3Ge(SO4)2(OH)6·3H2O

2013 ◽  
Vol 69 (2) ◽  
pp. i6-i6 ◽  
Author(s):  
Marcus J. Origlieri ◽  
Robert T. Downs
Keyword(s):  
Crystal Structure ◽  
Hydrogen Bonds ◽  
Structure Determination ◽  
Site Symmetry ◽  
Asymmetric Unit ◽  
Natural Sample ◽  
X Ray Diffraction ◽  
Full Matrix ◽  
X Ray

This report presents the first crystal structure determination of the mineral schaurteite, ideally Ca3Ge(SO4)2(OH)6·3H2O, tricalcium germanium bis(sulfate) hexahydroxide trihydrate. This single-crystal X-ray diffraction study investigated a natural sample from the type locality at Tsumeb, Namibia. Schaurteite is a member of the fleischerite group of minerals, which also includes fleischerite, despujolsite, and mallestigite. The structure of schaurteite consists of slabs of Ca(O,OH,H2O)8polyhedra (site symmetrymm2) interleaved with a mixed layer of Ge(OH)6octahedra (-3m.) and SO4tetrahedra (3m.). There are two H atoms in the asymmetric unit, both located by full-matrix refinement, and both forming O—H...O hydrogen bonds.

Isomorphous replacement in electron diffraction of wet crystals of rat hemoglobin

1983 ◽  
Vol 41 ◽  
pp. 446-447
Author(s):  
William F. Tivol ◽  
Murray Vernon King ◽  
D. F. Parsons
Keyword(s):  
Electron Diffraction ◽  
Heavy Atom ◽  
Isomorphous Substitution ◽  
X Ray Diffraction ◽  
Salt Solutions ◽  
X Ray ◽  
Isomorphous Replacement ◽  
Structure Factors ◽  
Diffraction Structure ◽  
The Mean

Feasibility of isomorphous substitution in electron diffraction is supported by a calculation of the mean alteration of the electron-diffraction structure factors for hemoglobin crystals caused by substituting two mercury atoms per molecule, following Green, Ingram & Perutz, but with allowance for the proportionality of f to Z3/4 for electron diffraction. This yields a mean net change in F of 12.5%, as contrasted with 22.8% for x-ray diffraction.Use of the hydration chamber in electron diffraction opens prospects for examining many proteins that yield only very thin crystals not suitable for x-ray diffraction. Examination in the wet state avoids treatments that could cause translocation of the heavy-atom labels or distortion of the crystal. Combined with low-fluence techniques, it enables study of the protein in a state as close to native as possible.We have undertaken a study of crystals of rat hemoglobin by electron diffraction in the wet state. Rat hemoglobin offers a certain advantage for hydration-chamber work over other hemoglobins in that it can be crystallized from distilled water instead of salt solutions.

Examination of Rabbit Fc Crystals

1968 ◽  
Vol 26 ◽  
pp. 140-141
Author(s):  
J. P. Robinson ◽  
P. G. Lenhert
Keyword(s):  
Molecular Weight ◽  
Flat Plate ◽  
Phosphate Buffer ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
X Ray ◽  
Neutral Ph ◽  
Small Crystals ◽  
Carbon Coated ◽  
Diffraction Patterns

Crystallographic studies of rabbit Fc using X-ray diffraction patterns were recently reported. The unit cell constants were reported to be a = 69. 2 A°, b = 73. 1 A°, c = 60. 6 A°, B = 104° 30', space group P21, monoclinic, volume of asymmetric unit V = 148, 000 A°3. The molecular weight of the fragment was determined to be 55, 000 ± 2000 which is in agreement with earlier determinations by other methods.Fc crystals were formed in water or dilute phosphate buffer at neutral pH. The resulting crystal was a flat plate as previously described. Preparations of small crystals were negatively stained by mixing the suspension with equal volumes of 2% silicotungstate at neutral pH. A drop of the mixture was placed on a carbon coated grid and allowed to stand for a few minutes. The excess liquid was removed and the grid was immediately put in the microscope.

Sem and X-Ray Analysis of Renal and Biliary Calculi

1976 ◽  
Vol 34 ◽  
pp. 306-307
Author(s):  
R. J. Narconis ◽  
G. L. Johnson
Keyword(s):  
Chemical Constituents ◽  
Natural State ◽  
X Ray Diffraction ◽  
Chemical Methods ◽  
X Ray ◽  
Additional Dimension ◽  
Biliary Calculi ◽  
Calculus Formation ◽  
Scanning Electron

Analysis of the constituents of renal and biliary calculi may be of help in the management of patients with calculous disease. Several methods of analysis are available for identifying these constituents. Most common are chemical methods, optical crystallography, x-ray diffraction, and infrared spectroscopy. The application of a SEM with x-ray analysis capabilities should be considered as an additional alternative.A scanning electron microscope equipped with an x-ray “mapping” attachment offers an additional dimension in its ability to locate elemental constituents geographically, and thus, provide a clue in determination of possible metabolic etiology in calculus formation. The ability of this method to give an undisturbed view of adjacent layers of elements in their natural state is of advantage in determining the sequence of formation of subsequent layers of chemical constituents.

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