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Approach of Serial Crystallography II
Serial crystallography (SX) is an emerging X-ray crystallographic method for determining macromolecule structures. It can address concerns regarding the limitations of data collected by conventional crystallography techniques, which require cryogenic ...
Ki-Hyun Nam
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Serial crystallography (SX) is an emerging technique to determine macromolecules at room temperature. SX with a pump–probe experiment provides the time-resolved dynamics of target molecules.
Ki Hyun Nam
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Serial crystallography at synchrotrons and X-ray lasers [PDF]
Serial crystallography was developed for the use at free-electron lasers but the approach has recently also been adapted to synchrotron sources. Here we discuss how the synergy between the two X-ray sources will facilitate a wide application of the technique in microcrystallography, room-temperature structure determination and time-resolved studies.
Standfuss J, Spence J
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Room Temperature Serial Crystallography at Synchrotrons [PDF]
Serial Femtosecond Crystallography (SFX) is the most commonly used method for the emerging structure determination at X-ray free-electron lasers (FELs). The high peak brilliance of the FEL and the possibility of using femtosecond pulses afford use of nano-to-micron sized crystals in a diffraction-before-destruction approach for the acquisition of high ...
Sabine Botha +10 more
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Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis
An estimated half of all proteins contain a metal, with these being essential for a tremendous variety of biological functions. X-ray crystallography is the major method for obtaining structures at high resolution of these metalloproteins, but there are considerable challenges to obtain intact structures due to the effects of radiation damage.
Hough, Michael A, Owen, Robin L
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Macromolecular Serial Crystallography (Volume II)
The successful adaptation of the serial macromolecular crystallography approach at most 3rd generation synchrotron facilities allows a fruitful synergy between synchrotrons and XFELs that have accelerated the access and impact of this approach to an even
Jose M. Martin-Garcia
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The structure of Chlamydomonas LOV1 as revealed by time-resolved serial synchrotron crystallography. [PDF]
The photo-reaction of the LOV1 domain of the Chlamydomonas reinhardtii phototropin is investigated by room-temperature time-resolved serial crystallography. A covalent adduct forms between the C4a atom of the central flavin-mononucleotide chromophore and a protein cysteine. The structure of the adduct is very similar to that of LOV2 determined 23 years
Schmidt M.
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Serial crystallography (SX) technique using synchrotron X-ray allows the visualization of room-temperature crystal structures with low-dose data collection as well as time-resolved molecular dynamics.
Suk-Youl Park +4 more
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Time-resolved β-lactam cleavage by L1 metallo-β-lactamase
Metallo-β-lactamases cleave β-lactam moiety of many broadly used antibiotics. Here the authors captured mechanistic details of the enzyme catalyzed reaction using time-resolved xray synchrotron serial crystallography.
M. Wilamowski +12 more
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The ultrabright and ultrashort pulses produced at X-ray free electron lasers (XFELs) has enabled studies of crystallized molecular machines at work under ‘native’ conditions at room temperature by the so-called time-resolved serial femtosecond ...
Jose M. Martin-Garcia
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