scholarly journals Structure determination of an integral membrane protein at room temperature from crystalsin situ

2015 ◽  
Vol 71 (6) ◽  
pp. 1228-1237 ◽  
Author(s):  
Danny Axford ◽  
James Foadi ◽  
Nien-Jen Hu ◽  
Hassanul Ghani Choudhury ◽  
So Iwata ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Structure Determination ◽  
Room Temperature ◽  
Protein Structures ◽  
Integral Membrane Protein ◽  
Data Sets ◽  
X Ray Diffraction ◽  
Haemophilus Influenza

The structure determination of an integral membrane protein using synchrotron X-ray diffraction data collected at room temperature directly in vapour-diffusion crystallization plates (in situ) is demonstrated. Exposing the crystalsin situeliminates manual sample handling and, since it is performed at room temperature, removes the complication of cryoprotection and potential structural anomalies induced by sample cryocooling. Essential to the method is the ability to limit radiation damage by recording a small amount of data per sample from many samples and subsequently assembling the resulting data sets using specialized software. The validity of this procedure is established by the structure determination ofHaemophilus influenzaTehA at 2.3 Å resolution. The method presented offers an effective protocol for the fast and efficient determination of membrane-protein structures at room temperature using third-generation synchrotron beamlines.

Structure determination of fatty acid ester biofuels via in situ cryocrystallisation and single crystal X-ray diffraction

CrystEngComm ◽  
2019 ◽  
Vol 21 (1) ◽  
pp. 41-52 ◽  
Author(s):  
Siriyara Jagannatha Prathapa ◽  
Cara Slabbert ◽  
Manuel A. Fernandes ◽  
Andreas Lemmerer
Keyword(s):  
Crystal Structure ◽  
Fatty Acid ◽  
Fatty Acid Ester ◽  
Structure Determination ◽  
Homologous Series ◽  
Methyl Esters ◽  
X Ray Diffraction ◽  
X Ray

In situ cryocrystallisation enabled the crystal structure determination of a homologous series of low-melting n-alkyl methyl esters Cn−1H2n+1CO2CH3.

scholarly journals An automated platform for in situ serial crystallography at room temperature

IUCrJ ◽  
2020 ◽  
Vol 7 (6) ◽  
pp. 1009-1018
Author(s):  
Zhong Ren ◽  
Cong Wang ◽  
Heewhan Shin ◽  
Sepalika Bandara ◽  
Indika Kumarapperuma ◽  
...  
Keyword(s):  
Data Collection ◽  
Room Temperature ◽  
Protein Structures ◽  
Routine Data ◽  
Protein Crystals ◽  
X Ray Diffraction ◽  
X Ray ◽  
Serial Crystallography ◽  
Routine Data Collection

Direct observation of functional motions in protein structures is highly desirable for understanding how these nanomachineries of life operate at the molecular level. Because cryogenic temperatures are non-physiological and may prohibit or even alter protein structural dynamics, it is necessary to develop robust X-ray diffraction methods that enable routine data collection at room temperature. We recently reported a crystal-on-crystal device to facilitate in situ diffraction of protein crystals at room temperature devoid of any sample manipulation. Here an automated serial crystallography platform based on this crystal-on-crystal technology is presented. A hardware and software prototype has been implemented, and protocols have been established that allow users to image, recognize and rank hundreds to thousands of protein crystals grown on a chip in optical scanning mode prior to serial introduction of these crystals to an X-ray beam in a programmable and high-throughput manner. This platform has been tested extensively using fragile protein crystals. We demonstrate that with affordable sample consumption, this in situ serial crystallography technology could give rise to room-temperature protein structures of higher resolution and superior map quality for those protein crystals that encounter difficulties during freezing. This serial data collection platform is compatible with both monochromatic oscillation and Laue methods for X-ray diffraction and presents a widely applicable approach for static and dynamic crystallographic studies at room temperature.

scholarly journals The role of protein purification in the structure determination of an integral membrane protein

1996 ◽  
Vol 52 (a1) ◽  
pp. C141-C141
Author(s):  
G. McDermott ◽  
S. M. Prince ◽  
M. Z. Papiz ◽  
A. M. Hawthornthwaite-Lawless ◽  
A. A. Freer ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Purification ◽  
Structure Determination ◽  
Integral Membrane Protein

Characterization, luminescent properties, and crystal structure determination of [Pt(Ph2bipy)Cl2]

2016 ◽  
Vol 57 (8) ◽  
pp. 1773
Author(s):  
S. Shamaei ◽  
A. Heidari ◽  
V. Amani
Keyword(s):  
Structure Determination ◽  
Room Temperature ◽  
Diffraction Method ◽  
Luminescent Properties ◽  
Luminescence Spectroscopy ◽  
X Ray Diffraction ◽  
X Ray ◽  
Square Planar ◽  
Orange Solution

New complex [Pt(Ph2bipy)Cl2] (1) is obtained from the reaction of H2PtCl6×6H2O and 4,4'-diphenyl-2,2'-bipyridine (Ph2bipy) in a mixture of methanol, chloroform, and dimethyl sulfo­xide. Suitable crystals of 1 for the diffraction experiment are obtained by slow evaporation of the resulted orange solution at room temperature. This complex is characterized by elemental analysis, IR, 1H NMR, UV-Vis, and luminescence spectroscopy and its structure is studied by the single crystal X-ray diffraction method. X-ray structure determination shows that in the structure of this compound, the Pt(II) atom is four-coordinated in a distorted square-planar configuration by two nitrogen atoms from a bidentate 4,4'-diphenyl-2,2'-bipyridine ligand and two terminal chlorine atoms.

scholarly journals Determination of Patterson group symmetry from sparse multi-crystal data sets in the presence of an indexing ambiguity

2018 ◽  
Vol 74 (5) ◽  
pp. 405-410 ◽  
Author(s):  
Richard J. Gildea ◽  
Graeme Winter
Keyword(s):  
Polar Space ◽  
Group Symmetry ◽  
Data Sets ◽  
X Ray Diffraction ◽  
X Ray ◽  
Space Groups ◽  
Partial Data ◽  
Multiple Samples

Combining X-ray diffraction data from multiple samples requires determination of the symmetry and resolution of any indexing ambiguity. For the partial data sets typical of in situ room-temperature experiments, determination of the correct symmetry is often not straightforward. The potential for indexing ambiguity in polar space groups is also an issue, although methods to resolve this are available if the true symmetry is known. Here, a method is presented to simultaneously resolve the determination of the Patterson symmetry and the indexing ambiguity for partial data sets.

Single Crystal Growth of High-Pressure Phases of Ice and Salt Hydrate Far Below the Original Melting Point by Mixing Alcohol: Crystal Structure Determination of Magnesium Chloride Heptahydrate

2020 ◽  
Author(s):  
Keishiro Yamashita ◽  
Kazuki Komatsu ◽  
Hiroyuki Kagi
Keyword(s):  
Crystal Structure ◽  
High Pressure ◽  
Crystal Growth ◽  
Single Crystal ◽  
Room Temperature ◽  
Growth Technique ◽  
Salt Hydrate ◽  
X Ray

An crystal-growth technique for single crystal x-ray structure analysis of high-pressure forms of hydrogen-bonded crystals is proposed. We used alcohol mixture (methanol: ethanol = 4:1 in volumetric ratio), which is a widely used pressure transmitting medium, inhibiting the nucleation and growth of unwanted crystals. In this paper, two kinds of single crystals which have not been obtained using a conventional experimental technique were obtained using this technique: ice VI at 1.99 GPa and MgCl<sub>2</sub>·7H<sub>2</sub>O at 2.50 GPa at room temperature. Here we first report the crystal structure of MgCl2·7H2O. This technique simultaneously meets the requirement of hydrostaticity for high-pressure experiments and has feasibility for further in-situ measurements.

Photoluminescence Enhancement of CdS Nanocrystals Fabricated on Dithiocarbamate Functionalized PET Substrates

2012 ◽  
Vol 512-515 ◽  
pp. 1511-1515
Author(s):  
Chun Lin Zhao ◽  
Li Xing ◽  
Xiao Hong Liang ◽  
Jun Hui Xiang ◽  
Fu Shi Zhang ◽  
...  
Keyword(s):  
Room Temperature ◽  
Hexagonal Structure ◽  
Diffraction Measurement ◽  
X Ray Diffraction ◽  
Visible Absorption ◽  
X Ray ◽  
Cds Nanocrystals ◽  
Morphological Studies ◽  
Transmission Electron

Cadmium sulfide (CdS) nanocrystals (NCs) were self-assembled and in-situ immobilized on the dithiocarbamate (DTCs)-functionalized polyethylene glycol terephthalate (PET) substrates between the organic (carbon disulfide diffused in n-hexane) –aqueous (ethylenediamine and Cd2+ dissolved in water) interface at room temperature. Powder X-ray diffraction measurement revealed the hexagonal structure of CdS nanocrystals. Morphological studies performed by scanning electron microscopy (SEM) and high-resolution transmission electron microscope (HRTEM) showed the island-like structure of CdS nanocrystals on PET substrates, as well as energy-dispersive X-ray spectroscopy (EDS) confirmed the stoichiometries of CdS nanocrystals. The optical properties of DTCs modified CdS nanocrystals were thoroughly investigated by ultraviolet-visible absorption spectroscopy (UV-vis) and fluorescence spectroscopy. The as-prepared DTCs present intrinsic hydrophobicity and strong affinity for CdS nanocrystals.

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