A DANTE tagging sequence for the evaluation of translational sample motion

1990 ◽  
Vol 15 (2) ◽  
pp. 334-339 ◽  
Author(s):  
Timothy J. Mosher ◽  
Michael B. Smith
Keyword(s):  
Sample Motion

4D in in vivo 2-photon laser scanning fluorescence microscopy with sample motion in 6 degrees of freedom

2011 ◽  
Vol 200 (1) ◽  
pp. 47-53 ◽  
Author(s):  
Sabine Scheibe ◽  
Mario M. Dorostkar ◽  
Christian Seebacher ◽  
Rainer Uhl ◽  
Frank Lison ◽  
...  
Keyword(s):  
Fluorescence Microscopy ◽  
Laser Scanning ◽  
Degrees Of Freedom ◽  
Sample Motion ◽  
6 Degrees Of Freedom

scholarly journals Consideration of sample motion in cryo-tomography based on alignment residual interpolation

2019 ◽  
Vol 205 (3) ◽  
pp. 1-6 ◽  
Author(s):  
Jose-Jesus Fernandez ◽  
Sam Li ◽  
David A. Agard
Keyword(s):  
Sample Motion

Is your cold-stream working for you or against you? An in-depth look at temperature and sample motion

2008 ◽  
Vol 41 (6) ◽  
pp. 1122-1133 ◽  
Author(s):  
R. W. Alkire ◽  
N. E. C. Duke ◽  
F. J. Rotella
Keyword(s):  
Temperature Profile ◽  
Gaseous Nitrogen ◽  
Alignment Tool ◽  
Final Data ◽  
Force Profile ◽  
Cold Stream ◽  
Sample Motion ◽  
The Impact ◽  
Lysozyme Crystals ◽  
Nozzle Opening

It is normally assumed that a commercial gaseous nitrogen cold-stream provides a sample environment near 100 K and that the force of the cold-stream does not induce movement in the sample. As might be expected, the reality is much more complex. Here, an investigation of one cold-stream, starting with the temperature profile, is presented. Using silicon single crystals and flexible mounting loops, an approximate force/vibration profile of the cold-stream is obtained. Results indicate that the center of the temperature profile is offset from the position suggested by the manufacturer-supplied alignment tool and coincides with the area within the cold-stream that has the most consistent force profile. Tests indicate that this region is only about one-third of the width of the cold-stream nozzle opening. To verify that the results were relevant to protein crystallographic data collection, the impact of cold-stream position on the final data quality for lysozyme crystals was analyzed. On the basis of the observations it is recommended that users perform a temperature profile of their cold-streams to ensure proper alignment instead of relying only on the alignment tool for setup. In addition, suggestions are made on what users can look for in data processing to identify problems with loop movement and what users can do to minimize the impact of these problems on their experiments.

Fractional-sample motion compensation using generalized interpolation

2010 ◽  
Author(s):  
Haricharan Lakshman ◽  
Benjamin Bross ◽  
Heiko Schwarz ◽  
Thomas Wiegand
Keyword(s):  
Motion Compensation ◽  
Sample Motion

scholarly journals Rapid focus map surveying for whole slide imaging with continuous sample motion

2017 ◽  
Vol 42 (17) ◽  
pp. 3379 ◽  
Author(s):  
Jun Liao ◽  
Yutong Jiang ◽  
Zichao Bian ◽  
Bahareh Mahrou ◽  
Aparna Nambiar ◽  
...  
Keyword(s):  
Whole Slide Imaging ◽  
Sample Motion

scholarly journals Sample motion-insensitive, full-range, complex, spectral-domain optical-coherence tomography

2010 ◽  
Vol 35 (23) ◽  
pp. 3913 ◽  
Author(s):  
Stefan Zotter ◽  
Michael Pircher ◽  
Erich Götzinger ◽  
Teresa Torzicky ◽  
Marco Bonesi ◽  
...  
Keyword(s):  
Optical Coherence Tomography ◽  
Full Range ◽  
Spectral Domain ◽  
Optical Coherence ◽  
Sample Motion

Generalized Interpolation-Based Fractional Sample Motion Compensation

2013 ◽  
Vol 23 (3) ◽  
pp. 455-466 ◽  
Author(s):  
Haricharan Lakshman ◽  
Heiko Schwarz ◽  
Thomas Wiegand
Keyword(s):  
Motion Compensation ◽  
Sample Motion

scholarly journals Multi-particle cryo-EM refinement with M visualizes ribosome-antibiotic complex at 3.7 Å inside cells

2020 ◽  
Author(s):  
Dimitry Tegunov ◽  
Liang Xue ◽  
Christian Dienemann ◽  
Patrick Cramer ◽  
Julia Mahamid
Keyword(s):  
Structure Determination ◽  
Software Tool ◽  
Series Data ◽  
Bacterial Cells ◽  
Sample Motion ◽  
70S Ribosome ◽  
Tilt Series ◽  
Particle Refinement

Cryo-electron microscopy (cryo-EM) enables macromolecular structure determination in vitro and in situ. In addition to aligning individual particles, accurate registration of sample motion and 3D deformation during exposures is crucial for achieving high resolution. Here we describe M, a software tool that establishes a reference-based, multi-particle refinement framework for cryo-EM data and improves the results of structure determination. M provides a unified optimization framework for both in vitro frame series and in situ tomographic tilt series data. We show that tilt series data can provide the same resolution as frame series, indicating that the alignment step no longer limits the resolution obtainable from tomographic data. In combination with Warp and RELION, M improves upon previous methods, and resolves a 70S ribosome bound to an antibiotic inside bacterial cells at a nominal resolution of 3.7 Å. Thus, computational tools are now available to resolve structures from tomographic in situ cryo-EM data at residue level.

Sign in / Sign up

Export Citation Format

Share Document