Nature Search

Author Correction: Structural basis of tRNA recognition by the m³C RNA methyltransferase METTL6 in complex with SerRS seryl-tRNA synthetase

Philipp Throll
Luciano G. Dolce
Eva Kowalinski
Amendments and CorrectionsOpen Access04 Feb 2025
Nature Structural & Molecular Biology

Volume: 32, P: 405
Author Correction: Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3

Luigi Scietti
Antonella Chiapparino
Federico Forneris
Amendments and CorrectionsOpen Access20 Sept 2018
Nature Communications

Volume: 9, P: 1
Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser

Femtosecond X-ray pulses were used to obtain diffraction data on photosystem II, revealing conformational changes as the complex transitions from the dark S₁ state to the double-pumped S₃ state; the time-resolved serial femtosecond crystallography technique enables structural determination of protein conformations that are highly prone to traditional radiation damage.

Christopher Kupitz
Shibom Basu
Petra Fromme
Research09 Jul 2014
Nature

Volume: 513, P: 261-265
Structural basis of tRNA recognition by the m³C RNA methyltransferase METTL6 in complex with SerRS seryl-tRNA synthetase

The authors use cryo-electron microscopy and biochemistry to reveal how 3-methylcytosine (m³C) methyltransferases bind tRNA. They also find that the human m³C methyltransferase METTL6 forms a tRNA-dependent complex with seryl-tRNA synthetase to methylate target tRNAs efficiently.

Philipp Throll
Luciano G. Dolce
Eva Kowalinski
ResearchOpen Access25 Jun 2024
Nature Structural & Molecular Biology

Volume: 31, P: 1614-1624
Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy

Alkaline ceramidases (ACERs) are a class of poorly understood transmembrane enzymes controlling the homeostasis of ceramides. Here authors solve the Xray structure of human ACER3 and uncover a Ca2+ binding site providing an explanation for the known regulatory role of Ca2+ on ACER3 activity.

Ieva Vasiliauskaité-Brooks
Robert D. Healey
Sébastien Granier
ResearchOpen Access21 Dec 2018
Nature Communications

Volume: 9, P: 1-13
Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography

Serial femtosecond X-ray crystallography permits the use of very small protein crystals; however, a continuous flow of sample is required. Weierstall et al. design and demonstrate an injector system that can supply microcrystals in the lipidic cubic phase, dramatically reducing the quantities of protein required.

Uwe Weierstall
Daniel James
Vadim Cherezov
Research14 Feb 2014
Nature Communications

Volume: 5, P: 1-6
Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons

Serial crystallography was developed for protein crystal data collection with X-ray free-electron lasers. Here the authors present several examples which show that serial crystallography using high-viscosity injectors can also be routinely employed for room-temperature data collection at synchrotrons.

Tobias Weinert
Natacha Olieric
Jörg Standfuss
ResearchOpen Access14 Sept 2017
Nature Communications

Volume: 8, P: 1-11
Ternary structure reveals mechanism of a membrane diacylglycerol kinase

Diacylglycerol kinase is a small bacterial membrane-bound trimer that catalyses diacylglycerol conversion to phosphatidic acid. Here, the authors solve the crystal structure of the kinase bound to a lipid substrate and an ATP analogue, and show that the active site arose through convergent evolution.

Dianfan Li
Phillip J. Stansfeld
Martin Caffrey
ResearchOpen Access17 Dec 2015
Nature Communications

Volume: 6, P: 1-12
Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3

Lysyl hydroxylase 3 (LH3) catalyzes collagen lysine hydroxylation and their subsequent O-linked glycosylation. Here the authors provide mechanistic insights into the lysyl hydroxylase and glycosyltransferase activities of LH3 by determining the crystal structures of full-length human LH3 bound to cofactors and donor substrates.

Luigi Scietti
Antonella Chiapparino
Federico Forneris
ResearchOpen Access08 Aug 2018
Nature Communications

Volume: 9, P: 1-11
Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser

G protein-coupled receptors are a large family of signalling proteins that mediate cellular responses primarily via G proteins or arrestins, and they are targets of one-third of the current clinically used drugs; here, an active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin-1 is determined, revealing unique structural features that may constitute essential elements for arrestin-biased signalling.

Yanyong Kang
X. Edward Zhou
H. Eric Xu
Research22 Jul 2015
Nature

Volume: 523, P: 561-567
Structural basis for bifunctional peptide recognition at human δ-opioid receptor

Serial femtosecond crystallography of the human δ-opioid receptor in complex with an endomorphin-derived peptide reveals interactions that are important for understanding the pharmacology of opioid peptides and developing analgesics with reduced side effects.

Gustavo Fenalti
Nadia A Zatsepin
Vadim Cherezov
Research16 Feb 2015
Nature Structural & Molecular Biology

Volume: 22, P: 265-268
Correction: Corrigendum: Diffraction data of core-shell nanoparticles from an X-ray free electron laser

Xuanxuan Li
Chun-Ya Chiu
Haiguang Liu
Amendments and CorrectionsOpen Access24 Oct 2017
Scientific Data

Volume: 4, P: 1
Macromolecular diffractive imaging using imperfect crystals

Crystal lattice disorder, which gives rise to a continuous diffraction pattern, is exploited to determine the structure of the integral membrane protein complex photosystem II to a higher resolution than could be achieved using Bragg diffraction alone.

Kartik Ayyer
Oleksandr M. Yefanov
Henry N. Chapman
Research10 Feb 2016
Nature

Volume: 530, P: 202-206
Free-electron laser data for multiple-particle fluctuation scattering analysis

Kanupriya Pande
Jeffrey J. Donatelli
Petrus H. Zwart
ResearchOpen Access02 Oct 2018
Scientific Data

Volume: 5, P: 1-7
Advancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron

Serial macromolecular crystallography has become a powerful method to reveal room-temperature structures of biological macromolecules and perform time-resolved studies, however, the experiments remain complex and challenging for broader applications. Here, the authors develop serial microsecond crystallography using high-brilliance, high-repetition-rate X-ray pulses at the newly constructed ID29 beamline of the ESRF-EBS 4th generation synchrotron, featuring microsecond exposure times, innovative beam characteristics, adaptable sample environment, and high-quality complete data.

Julien Orlans
Samuel L. Rose
Daniele de Sanctis
ResearchOpen Access07 Jan 2025
Communications Chemistry

Volume: 8, P: 1-12
Diffraction data of core-shell nanoparticles from an X-ray free electron laser

Xuanxuan Li
Chun-Ya Chiu
Haiguang Liu
ResearchOpen Access11 Apr 2017
Scientific Data

Volume: 4, P: 1-8
In situ serial crystallography for rapid de novo membrane protein structure determination

Huang et al. report a fully automated method for collecting and merging data from thousands of in meso-grown microcrystals. This in situ approach provides a fast and efficient way to determine the structures of membrane proteins from fragile microcrystals.

Chia-Ying Huang
Vincent Olieric
Meitian Wang
ResearchOpen Access27 Aug 2018
Communications Biology

Volume: 1, P: 1-8
Serial femtosecond crystallography datasets from G protein-coupled receptors

Thomas A. White
Anton Barty
Vadim Cherezov
ResearchOpen Access01 Aug 2016
Scientific Data

Volume: 3, P: 1-9

Search

Filter By:

Search

Quick links