scholarly journals X-CHIP: an integrated platform for high-throughput protein crystallization and on-the-chip X-ray diffraction data collection

2011 ◽  
Vol 67 (6) ◽  
pp. 533-539 ◽  
Author(s):  
Gera Kisselman ◽  
Wei Qiu ◽  
Vladimir Romanov ◽  
Christine M. Thompson ◽  
Robert Lam ◽  
...  
Keyword(s):  
Data Collection ◽  
High Throughput ◽  
Diffraction Data ◽  
Protein Crystallization ◽  
X Ray Diffraction ◽  
X Ray ◽  
Integrated Platform

A reliable methodology for high throughput identification of a mixture of crystallographic phases from powder X-ray diffraction data

CrystEngComm ◽  
2008 ◽  
Vol 10 (10) ◽  
pp. 1321 ◽  
Author(s):  
Laurent Allan Baumes ◽  
Manuel Moliner ◽  
Nicolas Nicoloyannis ◽  
Avelino Corma
Keyword(s):  
High Throughput ◽  
Diffraction Data ◽  
X Ray Diffraction ◽  
X Ray

Macromolecular crystallography at LURE: instrumentation for X-ray diffraction data collection and results

1993 ◽  
Vol 49 (s1) ◽  
pp. c11-c11
Author(s):  
R. Fourme ◽  
R. Kahn ◽  
W. Shepard ◽  
A. Beniley
Keyword(s):  
Data Collection ◽  
Diffraction Data ◽  
Macromolecular Crystallography ◽  
X Ray Diffraction ◽  
X Ray

Masquerade: removing non-sample scattering from integrated reflection intensities

2012 ◽  
Vol 45 (2) ◽  
pp. 292-298 ◽  
Author(s):  
J. A. Coome ◽  
A. E. Goeta ◽  
J. A. K. Howard ◽  
M. R. Probert
Keyword(s):  
Data Collection ◽  
Diffraction Data ◽  
Low Temperatures ◽  
Test Case ◽  
X Rays ◽  
Atmospheric Conditions ◽  
X Ray Diffraction ◽  
New Approach ◽  
X Ray ◽  
Internal Agreement

X-ray diffraction experiments at very low temperatures require samples to be isolated from atmospheric conditions and held under vacuum. These conditions are usually maintainedviathe use of beryllium chambers, which also scatter X-rays, causing unwanted contamination of the sample's diffraction pattern. The removal of this contamination requires novel data-collection and processing procedures to be employed. Herein a new approach is described, which utilizes the differences in origin of scattering vectors from the sample and the beryllium to eliminate non-sample scattering. The programMasqueradehas been written to remove contaminated regions of the diffraction data from the processing programs. Coupled with experiments at different detector distances, it allows for the acquisition of decontaminated data. Studies of several single crystals have shown that this approach increases data quality, highlighted by the improvement in internal agreement factor with the test case of cytidine presented herein.

scholarly journals The finer things in X-ray diffraction data collection

1999 ◽  
Vol 55 (10) ◽  
pp. 1718-1725 ◽  
Author(s):  
J. W. Pflugrath
Keyword(s):  
Data Collection ◽  
Diffraction Data ◽  
Rotation Angle ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
Software Suite ◽  
X Ray ◽  
Position Sensitive ◽  
X Ray Background ◽  
Position Sensitive Detectors

X-ray diffraction images from two-dimensional position-sensitive detectors can be characterized as thick or thin, depending on whether the rotation-angle increment per image is greater than or less than the crystal mosaicity, respectively. The expectations and consequences of the processing of thick and thin images in terms of spatial overlap, saturated pixels, X-ray background andI/σ(I) are discussed. Thed*TREKsoftware suite for processing diffraction images is briefly introduced, and results fromd*TREKare compared with those from another popular package.

The structure of cubic MOF [{Ca(H2O)6}{CaGd(oxydiacetate)3}2].4H2O. A comparison between structural models obtained from Rietveld refinement of conventional and synchrotron X-ray powder diffraction data and standard refinement of single-crystal X-ray diffraction data

2012 ◽  
Vol 27 (4) ◽  
pp. 232-242 ◽  
Author(s):  
Leopoldo Suescun ◽  
Jun Wang ◽  
Ricardo Faccio ◽  
Guzmán Peinado ◽  
Julia Torres ◽  
...  
Keyword(s):  
Data Collection ◽  
Single Crystal ◽  
Powder Diffraction ◽  
Diffraction Data ◽  
Structural Models ◽  
Initial Time ◽  
High Symmetry ◽  
Powder Diffraction Data ◽  
X Ray Diffraction ◽  
X Ray

The structure of the metal–organic framework (MOF) compound [{Ca(H2O)6}{CaGd(oxydiacetate)3}2]·4H2O was determined by single-crystal X-ray diffraction and refined using conventional single-crystal X-ray diffraction data. In addition, the structure was refined using powder diffraction data collected from two sources, a conventional X-ray diffractometer in Bragg–Brentano geometry and a 12-detector high resolution synchrotron-based diffractometer in transmission geometry. Data from the latter were processed in three different ways to account for crystalline decay or radiation damage. One dataset was obtained by averaging the multiple detector patterns, another dataset was obtained by cutting the non-overlapping portions of each detector to consider only the first few minutes of data collection and a dose-corrected dataset was obtained by fitting the independent peaks in every dataset and extrapolating the intensity and peak position to the initial time of data collection or to zero-absorbed dose. The compared structural models obtained show that special processing of powder diffraction data produced a much accurate model, close to the single-crystal-based model for this particular compound with heavy atoms in high symmetry positions that do not contribute to a significant number of diffraction intensities.

A geometrical approach for semi-automated crystal centering andin situX-ray diffraction data collection

2013 ◽  
Vol 46 (3) ◽  
pp. 740-745 ◽  
Author(s):  
Mohammad Yaser Heidari Khajepour ◽  
Hugo Lebrette ◽  
Xavier Vernede ◽  
Pierrick Rogues ◽  
Jean-Luc Ferrer
Keyword(s):  
Data Collection ◽  
High Throughput ◽  
Local Geometry ◽  
Geometrical Approach ◽  
Robot Arm ◽  
X Ray Diffraction ◽  
X Ray ◽  
Analysis Process ◽  
Handling Device

High-throughput protein crystallography projects pushed forward the development of automated crystallization platforms that are now commonly used. This created an urgent need for adapted and automated equipment for crystal analysis. However, first these crystals have to be harvested, cryo-protected and flash-cooled, operations that can fail or negatively impact on the crystal.In situX-ray diffraction analysis has become a valid alternative to these operations, and a growing number of users apply it for crystal screening and to solve structures. Nevertheless, even this shortcut may require a significant amount of beam time. In thisin situhigh-throughput approach, the centering of crystals relative to the beam represents the bottleneck in the analysis process. In this article, a new method to accelerate this process, by recording accurately the local geometry coordinates for each crystal in the crystallization plate, is presented. Subsequently, the crystallization plate can be presented to the X-ray beam by an automated plate-handling device, such as a six-axis robot arm, for an automated crystal centering in the beam,in situscreening or data collection. Here the preliminary results of such a semi-automated pipeline are reported for two distinct test proteins.

scholarly journals Use of the Bruker AXS SMART BREEZE™ System for Macromolecular X-ray Data Collection

2016 ◽  
Vol 13 (4) ◽  
Author(s):  
Christiana Standle ◽  
Blake Overson ◽  
Cody Black ◽  
Guizella Rocabado ◽  
Bruce Howard
Keyword(s):  
Data Collection ◽  
Diffraction Data ◽  
Undergraduate Research ◽  
Inorganic Compounds ◽  
Copper Anode ◽  
X Ray Diffraction ◽  
Small Unit ◽  
X Ray ◽  
Unit Cells ◽  
Protein Enzyme

The Bruker AXS SMART BREEZE™ system is a single-crystal X-ray diffractometer designed to collect data from crystals of small organic or inorganic compounds. It is typically equipped with a Molybdenum-anode sealed tube to facilitate data collection from small unit cells. We recently acquired this system, but chose to have it installed with a copper-anode sealed tube with the hope of using it to collect data from larger unit cells such as those found in crystals of proteins or other macromolecules. This is the first and only BREEZE™ system installed by Bruker AXS with a copper-anode to date. Here we show that this system is capable of efficiently collecting quality X-ray diffraction data from crystals of the enzymes lysozyme and xylanase. This capability to collect diffraction data from both macromolecular and small-molecule crystals greatly expands the scope of undergraduate research projects that can be addressed using this instrument. KEYWORDS: X-ray; Diffraction; Crystallography; Diffractometer; Protein; Enzyme; Crystal; Structure

scholarly journals Data-collection strategies

1999 ◽  
Vol 55 (10) ◽  
pp. 1703-1717 ◽  
Author(s):  
Zbigniew Dauter
Keyword(s):  
Data Collection ◽  
Information Content ◽  
Diffraction Data ◽  
Optimal Strategy ◽  
Reciprocal Lattice ◽  
Experimental Setup ◽  
X Ray Diffraction ◽  
X Ray ◽  
Factors Influencing ◽  
Collection Strategies

The optimal strategy for collecting X-ray diffraction data from macromolecular crystals is discussed. Two kinds of factors influencing the completeness of data are considered. The first are geometric, arising from the symmetry of the reciprocal lattice and from the experimental setup; they affect quantitatively the completeness of the measured set of reflections. The second concern the quality, or information content, of the recorded intensities of these measured reflections.

scholarly journals Visualisation of membrane protein crystals using X-ray imaging

2014 ◽  
Vol 70 (a1) ◽  
pp. C351-C351
Author(s):  
Anna Warren ◽  
Wes Armour ◽  
Danny Axford ◽  
Mark Basham ◽  
Thomas Connolley ◽  
...  
Keyword(s):  
Data Collection ◽  
Diffraction Data ◽  
Cubic Phase ◽  
Informed Decision Making ◽  
Macromolecular Crystallography ◽  
X Ray Diffraction ◽  
Shape Estimation ◽  
X Ray ◽  
Raster Scanning ◽  
X Ray Imaging

The focus in macromolecular crystallography is moving towards even more challenging target proteins that often crystallise on much smaller scales and are frequently mounted in opaque or highly refractive materials.[1,2] It is therefore essential that X-ray beamline technology develops in parallel to accommodate such difficult samples. In this poster the use of X-ray microradiography and microtomography is reported as a tool for crystal visualisation, location and characterization on the macromolecular crystallography beamlines at the Diamond Light Source. The technique is particularly useful for microcrystals, and crystals mounted in opaque materials such as lipidic cubic phase. X-ray diffraction raster scanning can be used in combination with radiography to allow informed decision-making at the beamline prior to diffraction data collection. It is demonstrated that the X-ray dose required for a full tomography measurement is similar to a diffraction grid scan. However, for sample location and shape estimation alone, just a few radiographic projections may be required; hence reducing the dose the crystals will be exposed to prior to the diffraction data collection.[3]

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