scholarly journals Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Stephen M. Keable ◽  
Adrian Kölsch ◽  
Philipp S. Simon ◽  
Medhanjali Dasgupta ◽  
Ruchira Chatterjee ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Photosystem I ◽  
Free Electron Laser ◽  
Room Temperature ◽  
Secondary Electron ◽  
Electron Acceptors ◽  
Parallel Orientation ◽  
X Ray ◽  
Symmetric Structure ◽  
Ps I

AbstractPhotosystem I (PS I) has a symmetric structure with two highly similar branches of pigments at the center that are involved in electron transfer, but shows very different efficiency along the two branches. We have determined the structure of cyanobacterial PS I at room temperature (RT) using femtosecond X-ray pulses from an X-ray free electron laser (XFEL) that shows a clear expansion of the entire protein complex in the direction of the membrane plane, when compared to previous cryogenic structures. This trend was observed by complementary datasets taken at multiple XFEL beamlines. In the RT structure of PS I, we also observe conformational differences between the two branches in the reaction center around the secondary electron acceptors A1A and A1B. The π-stacked Phe residues are rotated with a more parallel orientation in the A-branch and an almost perpendicular confirmation in the B-branch, and the symmetry breaking PsaB-Trp673 is tilted and further away from A1A. These changes increase the asymmetry between the branches and may provide insights into the preferential directionality of electron transfer.

scholarly journals Liquid sample delivery techniques for serial femtosecond crystallography

2014 ◽  
Vol 369 (1647) ◽  
pp. 20130337 ◽  
Author(s):  
Uwe Weierstall
Keyword(s):  
Flow Rate ◽  
Free Electron ◽  
Repetition Rate ◽  
Free Electron Laser ◽  
Room Temperature ◽  
Liquid Flow Rate ◽  
Free Electron Lasers ◽  
Liquid Sample ◽  
X Ray ◽  
Serial Femtosecond Crystallography

X-ray free-electron lasers overcome the problem of radiation damage in protein crystallography and allow structure determination from micro- and nanocrystals at room temperature. To ensure that consecutive X-ray pulses do not probe previously exposed crystals, the sample needs to be replaced with the X-ray repetition rate, which ranges from 120 Hz at warm linac-based free-electron lasers to 1 MHz at superconducting linacs. Liquid injectors are therefore an essential part of a serial femtosecond crystallography experiment at an X-ray free-electron laser. Here, we compare different techniques of injecting microcrystals in solution into the pulsed X-ray beam in vacuum. Sample waste due to mismatch of the liquid flow rate to the X-ray repetition rate can be addressed through various techniques.

5d and 4f electron configuration of CeB6 at 340 and 535 K

2008 ◽  
Vol 64 (5) ◽  
pp. 534-549 ◽  
Author(s):  
Ryoko Makita ◽  
Kiyoaki Tanaka ◽  
Yoshichika Ōnuki
Keyword(s):  
Electron Transfer ◽  
Crystal Field ◽  
Ground State ◽  
Room Temperature ◽  
Atomic Orbital ◽  
Energy Levels ◽  
Electron Configuration ◽  
Acta Cryst ◽  
X Ray ◽  
The Difference

X-ray atomic orbital (XAO) analysis revealed that at both temperatures the electrons are transferred from B 2px (= py ) to Ce 5d and 4f orbitals. At 340 K 5d(j = 5/2)Γ8 orbitals are occupied partially, but 4f(j = 5/2)Γ8 orbitals are more populated than 4f(j = 5/2)Γ7 orbitals, in contrast to our observation at 430 K [Makita et al. (2007). Acta Cryst. B63, 683–692]. At 535 K the XAO analysis revealed clearly that the order of the energy levels of 4f(j = 5/2)Γ8 and Γ7 states reversed again and is the same as that at room temperature. It also limited the possible 5d configurations to three models among the nine possible ones. However, the XAO analysis could not decide which of the three models was the best with the present accuracy of the measurement. Two of them have partially and fully occupied 5d(j = 5/2)Γ7 orbitals and the remaining one has a fully occupied 5d(j = 3/2)Γ8 orbital. Since the lobes of 5d(j = 3/2)Γ8 or 5d(j = 5/2)Γ7 orbitals do not overlap with the 4f(j = 5/2)Γ8 orbitals as well as the 5d(j = 5/2)Γ8 orbitals, the order of the energy levels of the 4f(j = 5/2) orbitals became the same as that at room temperature. These results indicate that the crystal field varies with temperature due to the electron transfer from B 2p to Ce 5d orbitals. The difference densities after the spherical-atom refinement at the three temperatures clearly revealed the different combinations of 4f and 5d orbitals which are occupied. In the present study positive peaks due to the 4f electrons appear near the Ce nucleus and those due to 5d orbitals are found in the area outside the 4f peaks. Between the two areas there is a negative area distributed spherically at 340 K. The negative area produced by the contraction of 4f(j = 5/2)Γ8 orbitals seems to reduce the electron repulsion of the 5d(j = 5/2)Γ8 orbitals and helps the 4f(j = 5/2)Γ8 orbitals to remain as the ground state.

Determination of x-ray free electron laser power using a room-temperature calorimeter

Metrologia ◽  
2016 ◽  
Vol 53 (1) ◽  
pp. 98-102 ◽  
Author(s):  
T Tanaka ◽  
M Kato ◽  
N Saito ◽  
K Tono ◽  
M Yabashi ◽  
...  
Keyword(s):  
Free Electron ◽  
Free Electron Laser ◽  
Laser Power ◽  
Room Temperature ◽  
X Ray

scholarly journals The Mn 4 Ca photosynthetic water-oxidation catalyst studied by simultaneous X-ray spectroscopy and crystallography using an X-ray free-electron laser

2014 ◽  
Vol 369 (1647) ◽  
pp. 20130324 ◽  
Author(s):  
Rosalie Tran ◽  
Jan Kern ◽  
Johan Hattne ◽  
Sergey Koroidov ◽  
Julia Hellmich ◽  
...  
Keyword(s):  
Free Electron ◽  
Water Oxidation ◽  
Free Electron Laser ◽  
Room Temperature ◽  
Oxidation Catalyst ◽  
Cryogenic Temperatures ◽  
New Approach ◽  
X Ray ◽  
The Past ◽  
Photosynthetic Water Oxidation

The structure of photosystem II and the catalytic intermediate states of the Mn 4 CaO 5 cluster involved in water oxidation have been studied intensively over the past several years. An understanding of the sequential chemistry of light absorption and the mechanism of water oxidation, however, requires a new approach beyond the conventional steady-state crystallography and X-ray spectroscopy at cryogenic temperatures. In this report, we present the preliminary progress using an X-ray free-electron laser to determine simultaneously the light-induced protein dynamics via crystallography and the local chemistry that occurs at the catalytic centre using X-ray spectroscopy under functional conditions at room temperature.

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