151. |
- Andersson, Greger, 1958-
(författare)
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What fish swallowed Jonah?
- 2005
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Ingår i: Fact and fiction in narrative. - Örebro : University Library, Örebro Universitet. - 9176684253 ; , s. 115-139
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Bokkapitel (övrigt vetenskapligt/konstnärligt)
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152. |
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153. |
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154. |
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155. |
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156. |
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157. |
- Andersson, Öivind, et al.
(författare)
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Crank Angle Resolved HC Detection Using LIF in the Exhausts of Small Two-Stroke Engines Running at High Engine Speed
- 1996
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Ingår i: SAE Transactions, Journal of Engines. - 0096-736X. ; 105:961927
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Tidskriftsartikel (refereegranskat)abstract
- In order to separate the HC-emissions from two-stroke engines into short-circuit losses and emissions due to incomplete combustion, Laser Induced Fluorescence (LIF) measurements were performed on the exhaust gases just outside the exhaust ports of two engines of different designs. The difference between the two engines was the design of the transfer channels. One engine had "finger" transfer channels and one had "cup handle" transfer channels. Apart from that they were similar. The engine with "finger" transfer channels was earlier known to give more short-circuiting losses than the other engine, and that behavior was confirmed by these measurements. Generally, the results show that the emission of hydrocarbons has two peaks, one just after exhaust port opening and one late in the scavenging phase. The spectral information shows differences between the two peaks and it can be concluded that the latter peak is due to short-circuiting and the earlier due to incomplete combustion. The flow outside the exhaust port was measured with Laser Doppler Velocimetry (LDV). These measurements confirm the occurrence of two emission peaks.
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158. |
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159. |
- Båth, Petra, 1988, et al.
(författare)
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Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre
- 2022
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Ingår i: Acta Crystallographica Section D-Structural Biology. - : International Union of Crystallography (IUCr). - 2059-7983. ; 78, s. 698-708
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Tidskriftsartikel (refereegranskat)abstract
- Serial crystallography is a rapidly growing method that can yield structural insights from microcrystals that were previously considered to be too small to be useful in conventional X-ray crystallography. Here, conditions for growing microcrystals of the photosynthetic reaction centre of Blastochloris viridis within a lipidic cubic phase (LCP) crystallization matrix that employ a seeding protocol utilizing detergent-grown crystals with a different crystal packing are described. LCP microcrystals diffracted to 2.25 angstrom resolution when exposed to XFEL radiation, which is an improvement of 0.15 angstrom over previous microcrystal forms. Ubiquinone was incorporated into the LCP crystallization media and the resulting electron density within the mobile Q(B) pocket is comparable to that of other cofactors within the structure. As such, LCP microcrystallization conditions will facilitate time-resolved diffraction studies of electron-transfer reactions to the mobile quinone, potentially allowing the observation of structural changes associated with the two electron-transfer reactions leading to complete reduction of the ubiquinone ligand.
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160. |
- Dods, Robert, 1989, et al.
(författare)
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From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography.
- 2017
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Ingår i: Structure. - : Elsevier BV. - 1878-4186 .- 0969-2126. ; 25:9, s. 1461-1468
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Tidskriftsartikel (refereegranskat)abstract
- Serial protein crystallography was developed at X-ray free-electron lasers (XFELs) and is now also being applied at storage ring facilities. Robust strategies for the growth and optimization of microcrystals are needed to advance the field. Here we illustrate a generic strategy for recovering high-density homogeneous samples of microcrystals starting from conditions known to yield large (macro) crystals of the photosynthetic reaction center of Blastochloris viridis (RCvir). We first crushed these crystals prior to multiple rounds of microseeding. Each cycle of microseeding facilitated improvements in the RCvir serial femtosecond crystallography (SFX) structure from 3.3-Å to 2.4-Å resolution. This approach may allow known crystallization conditions for other proteins to be adapted to exploit novel scientific opportunities created by serial crystallography.
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