scholarly journals CREDO: a new general-purpose laboratory instrument for small-angle X-ray scattering

2014 ◽  
Vol 47 (5) ◽  
pp. 1749-1754 ◽  
Author(s):  
András Wacha ◽  
Zoltán Varga ◽  
Attila Bóta

The details of a newly constructed small-angle X-ray scattering instrument are presented. The geometry of the instrument is highly customizable, enabling it to address vastly different experimental situations from academic research to industrial problems. The high degree of motorization and automation compared to conventional laboratory-scale SAXS instruments facilitates the alignment and daily use. Data reduction routines are incorporated in the instrument control software, yielding fully corrected and calibrated results promptly after the end of measurements. Optimization of the fluxversus resolution balance can be done routinely for each measurement task. A wide, continuous range ofq= 4πsinθ/λ can be reached, from below 0.02 nm−1up to 30 nm−1, corresponding to periodic distances ofca 350 nm down to 0.2 nm. A few representative results obtained from samples of different research fields demonstrate the versatility of the instrument. Scattering curves are routinely calibrated into absolute units using a glassy carbon secondary standard. More information and recent developments can be found on the web page of the instrument at http://credo.ttk.mta.hu.

2018 ◽  
Vol 2 (1) ◽  
pp. 69-79 ◽  
Author(s):  
Martin A. Schroer ◽  
Dmitri I. Svergun

Small-angle X-ray scattering (SAXS) has become a streamline method to characterize biological macromolecules, from small peptides to supramolecular complexes, in near-native solutions. Modern SAXS requires limited amounts of purified material, without the need for labelling, crystallization, or freezing. Dedicated beamlines at modern synchrotron sources yield high-quality data within or below several milliseconds of exposure time and are highly automated, allowing for rapid structural screening under different solutions and ambient conditions but also for time-resolved studies of biological processes. The advanced data analysis methods allow one to meaningfully interpret the scattering data from monodisperse systems, from transient complexes as well as flexible and heterogeneous systems in terms of structural models. Especially powerful are hybrid approaches utilizing SAXS with high-resolution structural techniques, but also with biochemical, biophysical, and computational methods. Here, we review the recent developments in the experimental SAXS practice and in analysis methods with a specific focus on the joint use of SAXS with complementary methods.


2009 ◽  
Vol 206 (8) ◽  
pp. 1723-1726 ◽  
Author(s):  
J. M. Feldkamp ◽  
M. Kuhlmann ◽  
S. V. Roth ◽  
A. Timmann ◽  
R. Gehrke ◽  
...  

2020 ◽  
Vol 118 (3) ◽  
pp. 138a
Author(s):  
Ivan Rajkovic ◽  
Tsutomu Matsui ◽  
Ping Liu ◽  
Thomas M. Weiss

2018 ◽  
Vol 74 (a1) ◽  
pp. a259-a259
Author(s):  
Ivan Rajkovic ◽  
Tsutomu Matsui ◽  
Ping Liu ◽  
Thomas M. Weiss

2020 ◽  
Vol 42 (1) ◽  
pp. 36-42
Author(s):  
Melissa Gräwert ◽  
Dmitri Svergun

The Beginner's Guide series covers key techniques and offers the scientifically literate but not necessarily expert audience a background briefing on the underlying science of a technique that is (or will be) widely used in molecular bioscience. The series covers a mixture of techniques, including some that are well established amongst a subset of our readership but not necessarily familiar to those in different specialisms. This Beginner's Guide introduces solution small-angle X-ray scattering (SAXS). Solution small-angle X-ray scattering (SAXS) is a powerful technique, which is complementary to different bioanalytical and structural methods. With straightforward data collection procedures and minimal restrictions in sample environment, information on size, shape and conformational flexibility of biological macromolecules and complexes in near native solutions can be rapidly obtained. Here, we highlight the recent developments that have advanced SAXS to a versatile tool with the capability to enrich almost any biochemical study.


Author(s):  
A. Deschamps ◽  
L. David ◽  
M. Nicolas ◽  
F. Bley ◽  
F. Livet ◽  
...  

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