Max T B Clabbers
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Explore the profile of Max T B Clabbers including associated specialties, affiliations and a list of published articles.
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23
Citations
340
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Recent Articles
1.
Clabbers M, Hattne J, Martynowycz M, Gonen T
bioRxiv
. 2025 Mar;
PMID: 40060527
A favorable signal-to-noise ratio is essential for obtaining high-quality diffraction data in macromolecular electron crystallography. Inelastic scattering contributes significantly to the noise, reducing contrast between diffraction peaks and background, which...
2.
Clabbers M, Hattne J, Martynowycz M, Gonen T
Nat Commun
. 2025 Mar;
16(1):2247.
PMID: 40050283
High-resolution information is important for accurate structure modeling but is challenging to attain in macromolecular crystallography due to the rapid fading of diffracted intensities at increasing resolution. While direct electron...
3.
Nicolas W, Gillman C, Weaver S, Clabbers M, Shiriaeva A, Her A, et al.
Nat Protoc
. 2024 Dec;
PMID: 39706914
Microcrystal electron diffraction (MicroED) has advanced structural methods across a range of sample types, from small molecules to proteins. This cryogenic electron microscopy (cryo-EM) technique involves the continuous rotation of...
4.
Clabbers M, Hattne J, Martynowycz M, Gonen T
bioRxiv
. 2024 Sep;
PMID: 39257752
High resolution information is important for accurate structure modelling. However, this level of detail is typically difficult to attain in macromolecular crystallography because the diffracted intensities rapidly fade with increasing...
5.
Hattne J, Clabbers M, Martynowycz M, Gonen T
Structure
. 2023 Nov;
31(12):1504-1509.e1.
PMID: 37992709
The combination of high sensitivity and rapid readout makes it possible for electron-counting detectors to record cryogenic electron microscopy data faster and more accurately without increasing the number of electrons...
6.
Hattne J, Clabbers M, Martynowycz M, Gonen T
bioRxiv
. 2023 Jul;
PMID: 37425889
The combination of high sensitivity and rapid readout makes it possible for electron-counting detectors to record cryogenic electron microscopy data faster and more accurately without increasing the exposure. This is...
7.
Martynowycz M, Shiriaeva A, Clabbers M, Nicolas W, Weaver S, Hattne J, et al.
Nat Commun
. 2023 Feb;
14(1):1086.
PMID: 36841804
Crystallizing G protein-coupled receptors (GPCRs) in lipidic cubic phase (LCP) often yields crystals suited for the cryogenic electron microscopy (cryoEM) method microcrystal electron diffraction (MicroED). However, sample preparation is challenging....
8.
Clabbers M, Martynowycz M, Hattne J, Gonen T
J Struct Biol X
. 2022 Dec;
6:100078.
PMID: 36507068
Microcrystal electron diffraction (MicroED) is a powerful technique utilizing electron cryo-microscopy (cryo-EM) for protein structure determination of crystalline samples too small for X-ray crystallography. Electrons interact with the electrostatic potential...
9.
Clabbers M, Martynowycz M, Hattne J, Nannenga B, Gonen T
J Struct Biol
. 2022 Aug;
214(4):107886.
PMID: 36044956
Microcrystal electron diffraction (MicroED) uses electron cryo-microscopy (cryo-EM) to collect diffraction data from small crystals during continuous rotation of the sample. As a result of advances in hardware as well...
10.
Gruene T, Clabbers M, Luebben J, Chin J, Reithofer M, Stowasser F, et al.
J Appl Crystallogr
. 2022 Jun;
55(Pt 3):647-655.
PMID: 35719299
Electron diffraction enables structure determination of organic small molecules using crystals that are too small for conventional X-ray crystallography. However, because of uncertainties in the experimental parameters, notably the detector...