Xylan, the second most abundant plant cell wall polysaccharide, is degraded by β‐xylanases and β‐xylosidases. Here, we present the 2.65 Å cryo‐EM structure of Enterobacter cloacae β‐xylosidase (EcXyl43, GH43) and the 2.4 Å X‐ray structure of its inactive F507A mutant.
Lorenzo Briganti +8 more
wiley +1 more source
Introduction to the virtual thematic issue on room-temperature biological crystallography
Roberto A. Steiner
doaj +1 more source
Data of fixed-target pink-beam serial synchrotron crystallography at the Pohang Light Source II. [PDF]
Kim Y, Nam KH.
europepmc +1 more source
When biology meets materials science – Interdisciplinary applications of electron microscopy
Abstract Research at the interface between biology and materials science creates challenges for electron microscopists. Everything from the sample preparation to the choice of imaging and analytical techniques and the interpretation of the resulting data refuses to sit comfortably within the domain of one discipline or the other.
Martin Saunders +5 more
wiley +1 more source
High-speed detectors enable synchrotron serial crystallography [PDF]
openaire +1 more source
Data of pink-beam serial synchrotron crystallography at the Pohang Light Source II. [PDF]
Kim Y, Nam KH.
europepmc +1 more source
Resolving polymorphs and radiation-driven effects in microcrystals using fixed-target serial synchrotron crystallography. [PDF]
Ebrahim A +8 more
europepmc +1 more source
Abstract This study provides the first petrographic, crystallographic, and chemical comparison between El Médano 300 (EM 300) and Northwest Africa 8155 (NWA 8155), two particular IAB‐ungrouped iron meteorites. Both contain exceptionally large graphite nodules and “flowers”, providing unique insights into carbon behavior in metallic melts and cooling ...
L. Perez +8 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. [PDF]
Gotthard G +14 more
europepmc +1 more source
Crystal Structure and Conformational Dynamics of N─N Bond‐Forming Piperazate Synthase
Piperazate synthases (PZSs) catalyze the key N─N bond formation in the biosynthesis of the rare amino acid piperazic acid. X‐ray crystal structures of apo‐ and holo‐SbPZS show a dimeric enzyme with two heme‐containing active sites, where histidine residues coordinate the iron centers.
Nikita Pal +7 more
wiley +1 more source

