Results 131 to 140 of about 3,647 (218)

MIDAS: a methodological framework for high‐speed high‐energy diffraction microscopy data reduction. Part I: methodology

open access: yesActa Crystallographica Section A, EarlyView.
This paper details the complete methodological framework implemented in the MIDAS software for processing high‐energy diffraction microscopy (HEDM) data. We describe the specific algorithms, coordinate systems and physical models used for both far‐field and near‐field HEDM analysis.
Hemant Sharma   +2 more
wiley   +1 more source

Crystallography in Open Science and its open educational resources

open access: yesActa Crystallographica Section A, EarlyView.
Open Science is the movement to make scientific research, the data and their dissemination available to any member of an inquiring society, from professionals to citizens, irrespective of their economic situation. The IUCr provides fully open educational resources to Global South and Global North readers and authors.This article presents a review of ...
John R. Helliwell
wiley   +1 more source

Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography. [PDF]

open access: yesNat Commun
Bosman R   +13 more
europepmc   +1 more source

Assessing protein‐specific radiation damage in time‐resolved X‐ray solution‐scattering experiments at high‐brilliance synchrotrons using fast detector readout

open access: yesActa Crystallographica Section D, EarlyView.
Adenylate kinase was used to quantify how experimental parameters influence radiation damage during time‐resolved X‐ray solution scattering (TR‐XSS) at a multipurpose SAXS beamline. The study provides general guidelines for minimizing radiation artifacts in TR‐XSS.Time‐resolved X‐ray solution scattering (TR‐XSS) enables tracking of protein structural ...
Fatemeh Sabzian-Molaei   +2 more
wiley   +1 more source

Biochemical and structural characterization of a tail‐spike protein with depolymerase activity identified in a marine podovirus

open access: yesActa Crystallographica Section D, EarlyView.
The marine tail‐spike protein Dpo31 degrades the exopolysaccharide of its host and has structural features similar to those of other members of this protein class, despite similarity not being detected at the sequence level.Marine phages are, through the infection of their bacterial hosts, key regulators of microbiome and carbon fluxes in the ocean ...
Serena Sirigu   +7 more
wiley   +1 more source

Structural basis of regioselective double halogenation of the β‐carboline tryptoline by the single‐component halogenase AetF

open access: yesActa Crystallographica Section D, EarlyView.
A structure of the flavin‐dependent single‐component tryptophan halogenase AetF bound to the non‐native tricyclic substrate tryptoline reveals a binding pose analogous to l‐tryptophan that directs C6‐first halogenation. Product analysis identifies 6,8‐dibromotryptoline as the final product.Flavin‐dependent halogenases (FDHs) offer a biocatalytic route ...
Simon Bork   +3 more
wiley   +1 more source

Capturing the blue-light activated state of the Phot-LOV1 domain from Chlamydomonas reinhardtii using time-resolved serial synchrotron crystallography

open access: yes, 2023
Gotthard G   +14 more
europepmc   +1 more source

Anemia‐associated mutations disrupt the CDIN1‐Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA‐I) disease

open access: yesThe FEBS Journal, EarlyView.
Congenital dyserythropoietic anemia type I (CDA‐I) arises from mutations in Codanin1 and CDIN1. Using quantitative biophysical approaches, we show that disease‐associated mutations disrupt the CDIN1‐Codanin1 complex. Our findings provide critical insights into the molecular mechanism that links protein dysfunction to disturbing chromatin arrangement ...
Martin Stojaspal   +8 more
wiley   +1 more source

Water, water, every where—the advent of hydrated pili structure

open access: yesThe FEBS Journal, EarlyView.
Protein structure is defined by its surrounding water. Naturally, this is also true for the gigantic protein filaments that pathogenic bacteria use to attach to and colonize their host cells. Structures of these filaments for which water can be identified with high confidence have stayed elusive for the longest time.
Hiroya Oki   +3 more
wiley   +1 more source

Unraveling the active site cover of coproheme decarboxylase from Listeria monocytogenes

open access: yesThe FEBS Journal, EarlyView.
During heme biosynthesis in Gram‐positive bacteria, coproheme decarboxylase (ChdC) catalyzes the conversion of four‐propionate substrate coproheme to the two propionate product heme b. Its active site is universally covered by a flexible linking loop. This study identifies an important histidine residue, which stabilizes the loop in a ChdC homolog.
Nikolaus Falb   +4 more
wiley   +1 more source

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