Modified Nextal crystallization device forin situinspection of protein crystal quality

2005 ◽  
Vol 38 (2) ◽  
pp. 396-397 ◽  
Author(s):  
Nobuhisa Watanabe

The modification and use of the Nextal crystallization device for checking the diffraction quality of protein crystalsin situis described. Using the modified device, crystals in the crystallization drop can be exposed to X-rays directly to observe the diffraction quality without physical damage to the crystal. If the crystals in the drop are well separated, not only the resolution limit of the crystal is estimated, but also determination of the space group and the cell parameters is possible.

2015 ◽  
Vol 70 (3) ◽  
pp. 191-196 ◽  
Author(s):  
Olaf Reckeweg ◽  
Francis J. DiSalvo

AbstractThe new compounds LiK[C(CN)3]2 and Li[C(CN)3]·½ (H3C)2CO were synthesized and their crystal structures were determined. Li[C(CN)3]·½ (H3C)2CO crystallizes in the orthorhombic space group Ima2 (no. 46) with the cell parameters a=794.97(14), b=1165.1(2) and c=1485.4(3) pm, while LiK[C(CN)3]2 adopts the monoclinic space group P21/c (no. 14) with the cell parameters a=1265.7(2), b=1068.0(2) and c=778.36(12) pm and the angle β=95.775(7)°. Single crystals of K[C(CN)3] were also acquired, and the crystal structure was refined more precisely than before corroborating earlier results.


2011 ◽  
Vol 17 (1) ◽  
pp. 107-115 ◽  
Author(s):  
Nada Babovic ◽  
Dejan Markovic ◽  
Vojkan Dimitrijevic ◽  
Dragan Markovic

This paper shows the results obtained in field analysis performed at the Tamis River, starting from the settlement Jasa Tomic - border between Serbia and Romania to Pancevo - confluence of Tamis into the Danube. The Tamis is a 359 km long river rising in the southern Carpathian Mountains. It flows through the Banat region and flows into the Danube near Pancevo. During the years the water quality of the river has severely deteriorated and badly affected the environment and the river ecosystem. In situ measurements enabled determination of physico-chemical parameters of water quality of the Tamis River on every 400 m of the watercourse, such as: water temperature, pH value, electrical conductivity, contents of dissolved oxygen and oxygen saturation. The main reason of higher pollution of Tamis is seen in connection to DTD hydro system. Sampling was performed at 7 points with regard to color, turbidity, total hardness, alkalinity, concentration of ammonium nitrogen, nitrite nitrogen, nitrate nitrogen, iron, chlorides and sulphates in samples. The aim of the present work was to evaluate water quality in the Tamis River taking into account significant pollution, which originates from settlements, industry and agriculture, and to suggest appropriate preventive measures to further pollution decreasing of the river's water.


1980 ◽  
Vol 35 (8) ◽  
pp. 1015-1018 ◽  
Author(s):  
Werner Winter ◽  
Hanspeter Bühl ◽  
Herbert Meier

Abstract Fragmentation of 1,2,3-thiadiazoles (1) leads to the compounds 5 - 8 with an increasing proportion of sulphur. Numerous structural possibilities exist for the products 7 with the general formula (R2C2)2S3. The number of proposals can be reduced by spectroscopic techniques, but the final structure determination is accomplished by an X-ray analysis of the title compound 7a. 7a crystallizes in the space group P21/c (Z = 4) with cell parameters of a = 9.714(1), b = 16.188(8), c = 9.149(2) Å and β = 98.93(1)°. The structure is solved by direct methods and refined to R = 0.053 with 1955 diffractometer data (I ≥ 2σ(I)). The trithiolane ring has a puckered conformation and the whole molecule shows nearly perfect C2-symmetry, which is not required crystallographically.


2014 ◽  
Vol 70 (a1) ◽  
pp. C1140-C1140
Author(s):  
James Holton

The ultimate test of any crystallization experiment is how well the crystals (if any) diffract x-rays. In particular, we would like this diffraction data to be as free from caveats as possible, so that we know one condition really does produce better crystals than another, and not that we had a great crystal somewhere, but it was messed up in the harvesting and cryo-preservation process. So why doesn't everyone do in-situ diffraction? The reason is because of background. The principle impediment to observing weak high-resolution spots is that they get lost in the background scattering, so every effort must be made to minimize it. Unfortunately, plastic, water, oil, amorphous protein and protein crystal all generate a similar number of background x-rays per unit thickness. This is because they are all made of similarly light elements (oxygen, carbon, nitrogen) and have similar densities (0.9 to 1.2 g/cm^3). There is no such thing as a "low background" material, and everything the main beam touches on its way in, through and out of whatever is holding the crystal generates background. This is why loop mounts are so popular: the total path of the x-rays through non-crystalline stuff in a typical loop mount is generally not much thicker than the crystal, and reducing this thickness further has diminishing returns because the background is now dominated by that from disorder in the crystal lattice itself. So, why not make ultra-thin in-situ trays? Not only are thin walls difficult to manufacture cheaply, but they also dry out a lot faster, which is problematic for growing the crystals in the first place. The future success of in-situ diffraction requires trays that are not only thin-walled and low-permeability, but cheap.


2010 ◽  
Vol 66 (6) ◽  
pp. 579-584 ◽  
Author(s):  
Kevin Robertson ◽  
David Bish

X-ray powder diffraction (XRD) data were used to solve the crystal structures of phases in the magnesium perchlorate hydrate system, Mg(ClO4)2·nH2O (n = 4, 2). A heating stage and humidity generator interfaced to an environmental cell enabled in-situ XRD analyses of dehydration reactions under controlled temperatures and partial pressures of H2O (P_{{\rm H}_2{\rm O}}). The crystal structures were determined using an ab initio charge-flipping method and were refined using fundamental-parameter Rietveld methods. Dehydration of magnesium perchlorate hexahydrate to tetrahydrate (348 K) results in a decrease in symmetry (space group = C2), where isolated Mg2+ cations are equatorially coordinated by four H2O molecules with two [ClO4]− tetrahedra at the apices. Further dehydration to the dihydrate (423 K) leads to bridging of the isolated packets to form double corner-sharing chains of octahedra and polyhedra (space group = C2/m).


2020 ◽  
Vol 84 (5) ◽  
pp. 699-704
Author(s):  
Luca Bindi ◽  
Andrew C. Roberts ◽  
Cristian Biagioni

AbstractAlstonite, BaCa(CO3)2, is a mineral described almost two centuries ago. It is widespread in Nature and forms magnificent cm-sized crystals. Notwithstanding, its crystal structure was still unknown. Here, we report the crystal-structure determination of the mineral and discuss it in relationship to other polymorphs of BaCa(CO3)2. Alstonite is trigonal, space group P31m, with unit-cell parameters a = 17.4360(6), c = 6.1295(2) Å, V = 1613.80(9) Å3 and Z = 12. The crystal structure was solved and refined to R1 = 0.0727 on the basis of 4515 reflections with Fo > 4σ(Fo) and 195 refined parameters. Alstonite is formed by the alternation, along c, of Ba-dominant and Ca-dominant layers, separated by CO3 groups parallel to {0001}. The main take-home message is to show that not all structure determinations of minerals/compounds can be solved routinely. Some crystals, even large ones displaying excellent diffraction quality, can be twinned in complex ways, thus making their study a crystallographic challenge.


Author(s):  
Janet Newman ◽  
Julie A. Sharp ◽  
Ashwantha Kumar Enjapoori ◽  
John Bentley ◽  
Kevin R. Nicholas ◽  
...  

Monotreme lactation protein (MLP) is a recently identified protein with antimicrobial activity. It is present in the milk of monotremes and is unique to this lineage. To characterize MLP and to gain insight into the potential role of this protein in the evolution of lactation, the crystal structure of duck-billed platypus (Ornithorhynchus anatinus) MLP was determined at 1.82 Å resolution. This is the first structure to be reported for this novel, mammalian antibacterial protein. MLP was expressed as a FLAG epitope-tagged protein in mammalian cells and crystallized readily, with at least three space groups being observed (P1,C2 andP21). A 1.82 Å resolution native data set was collected from a crystal in space groupP1, with unit-cell parametersa= 51.2,b= 59.7,c= 63.1 Å, α = 80.15, β = 82.98, γ = 89.27°. The structure was solved by SAD phasing using a protein crystal derivatized with mercury in space groupC2, with unit-cell parametersa= 92.7,b = 73.2,c= 56.5 Å, β = 90.28°. MLP comprises a monomer of 12 helices and two short β-strands, with much of the N-terminus composed of loop regions. The crystal structure of MLP reveals no three-dimensional similarity to any known structures and reveals a heretofore unseen fold, supporting the idea that monotremes may be a rich source for the identification of novel proteins. It is hypothesized that MLP in monotreme milk has evolved to specifically support the unusual lactation strategy of this lineage and may have played a central role in the evolution of these mammals.


2001 ◽  
Vol 222 (1-2) ◽  
pp. 110-117 ◽  
Author(s):  
H.Z Xu ◽  
K Takahashi ◽  
C.X Wang ◽  
Z.G Wang ◽  
Y Okada ◽  
...  

Author(s):  
Dustin J. Little ◽  
John C. Whitney ◽  
Howard Robinson ◽  
Patrick Yip ◽  
Mark Nitz ◽  
...  

The periplasmic poly-β-1,6-N-acetyl-D-glucosamine (PNAG) de-N-acetylase PgaB fromEscherichia coliwas overexpressed and purified, but was recalcitrant to crystallization. Use of thein situproteolysis technique produced crystals of PgaB, but these crystals could not be optimized for diffraction studies. By analyzing the initial crystal hits using SDS–PAGE and mass spectrometry, the boundaries of the protein species that crystallized were determined. The re-engineered protein target crystallized reproducibly without the addition of protease and with significantly increased crystal quality. Crystals of the selenomethionine-incorporated protein exhibited the symmetry of space groupP212121and diffracted to 2.1 Å resolution.


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