Alke Meents

Universität Hamburg

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Henry N. Chapman

Universität Hamburg

J. Lieske

Deutsches Elektronen-Synchrotron DESY

Oleksandr Yefanov

Center for Free-Electron Laser Science

P. Fischer

Deutsches Elektronen-Synchrotron DESY

P. Reinke

Deutsches Elektronen-Synchrotron DESY

D. Oberthüer

Universität Hamburg

Thomas J. Lane

SLAC National Accelerator Laboratory

A. Tolstikova

Center for Free-Electron Laser Science

Sven Falke

Universität Hamburg

Helen M. Ginn

Diamond Light Source

Cooperative Institutions

Universität Hamburg

287

Deutsches Elektronen-Synchrotron DESY

239

Center for Free-Electron Laser Science

180

European X-Ray Free-Electron Laser

119

Max Planck Institute for the Structure and Dynamics of Matter

Paul Scherrer Institute

SLAC National Accelerator Laboratory

Hamburg Centre for Ultrafast Imaging

Arizona State University

Centre National de la Recherche Scientifique

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X-ray crystal structure of HEWL flash-cooled at high pressure

Anja Burkhardt Martin Warmer S. Panneerselvam Armin Wagner Raylene A. Reimer

10.2210/pdb4a7d/pdb

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Single-shot pink beam serial crystallography: Phycocyanin (One chip, chip_1)

Alke Meents D. Oberthüer J. Lieske V. Šrajer Iosifina Sarrou

10.2210/pdb5mjq/pdb

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Crystal structure of tetraaquamanganese(II) selenate monohydrate, Mn(H2O)4SeO4 · H2O

Zeitschrift für Kristallographie - New Crystal Structures (2003)

H. Euler Alke Meents Bruno Barbier Α. Kirfel

H10MnO9Se, triclinic, P1 (No. 2), a = 6.471(3)Å, b = 10.898(3)Å, c = 6.263(4)Å, a = 81.45(2)°,b = 109.43(2)°,g = 104.37(3)°,V = 402.4Å 3 , Z = 2, Rgt(F) = 0.017, wRref(F 2 ) = 0.043, T = 293 K.

Triclinic crystal system

Selenate

10.1524/ncrs.2003.218.1.9

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Online dynamic flat-field correction for MHz microscopy data at European XFEL

Journal of Synchrotron Radiation (2023)

Šarlota Birnšteinová Danilo E. Ferreira de Lima E. V. Sobolev Henry Kirkwood Valerio Bellucci

The high pulse intensity and repetition rate of the European X-ray Free-Electron Laser (EuXFEL) provide superior temporal resolution compared with other X-ray sources. In combination with MHz X-ray microscopy techniques, it offers a unique opportunity to achieve superior contrast and spatial resolution in applications demanding high temporal resolution. In both live visualization and offline data analysis for microscopy experiments, baseline normalization is essential for further processing steps such as phase retrieval and modal decomposition. In addition, access to normalized projections during data acquisition can play an important role in decision-making and improve the quality of the data. However, the stochastic nature of X-ray free-electron laser sources hinders the use of standard flat-field normalization methods during MHz X-ray microscopy experiments. Here, an online ( i.e. near real-time) dynamic flat-field correction method based on principal component analysis of dynamically evolving flat-field images is presented. The method is used for the normalization of individual X-ray projections and has been implemented as a near real-time analysis tool at the Single Particles, Clusters, and Biomolecules and Serial Femtosecond Crystallography (SPB/SFX) instrument of EuXFEL.

Normalization

10.1107/s1600577523007336

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Low-background pink-beam serial crystallography

Acta Crystallographica Section A Foundations and Advances (2017)

Alke Meents Max O. Wiedorn V. Šrajer Robert H. Henning Iosifina Sarrou

10.1107/s0108767317096052

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Poster

De Gruyter eBooks (2021)

Hina Andaleeb Christian Betzel H. Brognaro Stephan Falke Nazif Ullah

Spatially resolved anomalous dispersion (SpReAD) refinement is a method to analyse the oxidation states of individual protein-bound metals and is based on collecting several x-ray diffraction datasets across an x-ray absorption edge.Such an approach can expose crystals to relatively high total dose of radiation.This can result in radiation damage, including reduction of metals.Here, we have conducted experiments for SpReAD analysis on HZB MX beamline 14.1.To analyse the effect of dose on the result of the experiments, we have tested different transmission settings to vary the total dose per experiment and test whether data collected at low transmission are suitable for SpReAD refinement.

10.1515/9783110740172-003

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A new understanding of radiation damage at cryogenic temperatures

Acta Crystallographica Section A Foundations of Crystallography (2008)

Alke Meents Sascha Gutmann Clemens Schulze‐Briese

Poster Sessions micro meter to 10 micro meter.Until now a protein crystal is picked up manually from a crystallization droplet using a cryoloop and is mounted on a goniometer head.However it seems to be impossible to manipulate the protein microcrystal by hands, because the protein microcrystals are very small and fragile against a shock.So we are developing an automatic microcrystal pick-up system.In the system, we applied optical tweezers to manipulate the fragile protein crystal.It was reported that the optical tweezers at the near-infrared region traps and manipulates a cell without critical photodamage.We tried two kinds of optics for optical tweezers.One had a condensing lens, the other had a lensed fiber probe, which focused the laser on the object.The optical tweezers with the condensing lens succeeded in trapping of protein crystals with the size in 100 micro meter range.X-ray measurement of the trapped crystals indicated that laser trap with 1064 nm wavelength hardly affected the result of X-ray structural analysis.On the other hand, the optical tweezers with the two lensed fiber probe could manipulate the protein microcrystal with lower emission power.The lensed fiber probe was smaller than former, which had an advantage to be operated in the crystallization droplets at various crystallization plates.

radiation damage

10.1107/s0108767308089964

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Structural elucidation and antiviral activity of cathepsin L inhibitors with carbonyl and epoxide warheads

bioRxiv (Cold Spring Harbor Laboratory) (2023)

Sven Falke J. Lieske Alexander Herrmann Jure Loboda Sebastian Günther

Abstract Emerging RNA viruses including SARS-CoV-2 continue to be a major threat around the globe. The cell entry of SARS-CoV-2 particles via the endosomal pathway involves the cysteine protease cathepsin L (CatL) among other proteases. CatL is rendered as a promising drug target in the context of different viral and lysosome-related diseases. Hence, drug discovery and structure-based optimization of inhibitors is of high pharmaceutical interest. We herein verified and compared the anti-SARS-CoV-2 activity of a set of carbonyl and succinyl-epoxide-based inhibitors, which have previously been identified as cathepsin inhibitors. Calpain inhibitor XII (CI-XII), MG-101 and CatL inhibitor IV (CLI-IV) possess antiviral activity in the very low nanomolar IC 50 range in Vero E6 cells. Experimental structural data on how these and related compounds bind to CatL are however notably lacking, despite their therapeutic potential. Consequently, we present and compare crystal structures of CatL in complex with 14 compounds, namely BOCA ( N -BOC-2-aminoacetaldehyde), CLI-IV, CI-III, CI-VI, CI-XII, the main protease α-ketoamide inhibitor 13b, MG-101, MG-132 as well as E-64d (aloxistatin), E-64, CLIK148, CAA0225, TC-I (CID 16725315) and TPCK at resolutions better than 2 Å. Overall, the presented data comprise a broad and solid basis for structure-guided understanding and optimization of CatL inhibitors towards protease drug development.

Cathepsin L

Cysteine protease

10.1101/2023.08.11.552671

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Transferring the entatic-state principle to copper photochemistry

Nature Chemistry (2018)

Benjamin Dicke Alexander Hoffmann Julia Stanek Michael S. Rampp Benjamin Grimm‐Lebsanft

Photoexcitation

Coordination geometry

Coordination complex

Picosecond