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226 results for “x-ray diffraction”

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zenodo44/100

Diffraction data underpinning the structure of StayGold determined by X-ray crystallography (PDB code 8BXT)

<p>Raw diffraction data underpinning the crystal structure of StayGold fluorescent protein.</p> <p>This is the raw data underpinning PDB entry 8BXT.</p>

opencc-by-4.0Sep 2023View details →
zenodo40/100

IODP Expedition 361 X-ray diffraction (XRD)

<p>X-ray diffraction (XRD) is used to identify minerals and their proportions in sediment or hard rock sample powders on a Bruker AXS D4 Endeavor X-ray diffractometer. Results are returned as diffractograms in a viewable format (either PDF or PNG).</p>

opencc-zeroJan 2020View details →
zenodo40/100

Time- and angle-resolved photoemission spectroscopy data and time-resolved X-ray diffraction data of TbTe3

<p>Time- and angle-resolved photoemission spectroscopy data of bulk terbium tritelluride (TbTe3, unidirectional charge-density-wave phase, T=100K) using a laser-based femtosecond XUV source and a hemispherical analyzer for photoelectron detection at the Fritz-Haber-Institute, Berlin, Germany. The 3D (angle, energy, pump-probe-delay) datasets include the photoemission intensities for various pump-laser fluences.</p> <p>The time-resolved X-ray diffraction data were&nbsp;obtained at the Femto hard X-ray slicing source at the Swiss Light Source, and include the charge-density-wave superlattice (2 10 1+q_CDW) peak intensities as functions of pump-probe-delay for various pump-laser fluences.</p> <p>The data and associated metadata are stored in the NeXus data format (https://www.nexusformat.org/).</p>

opencc-by-4.0Oct 2020View details →
zenodo40/100

IODP Expedition 368X X-ray diffraction (XRD)

<p>X-ray diffraction (XRD) is used to identify minerals and their proportions in sediment or hard rock sample powders on a Bruker AXS D4 Endeavor X-ray diffractometer. Results are returned as diffractograms in a viewable format (either PDF or PNG).</p>

opencc-zeroJan 2021View details →
zenodo40/100

X-ray diffraction images for human recombinant 5-aminolevulinic acid dehydratase (ALAD).

<p>X-ray diffraction images for recominant human 5-aminolevulinic acid dehydratase (ALAD) collected at ESRF (Grenoble) beam line ID14-2 using an ADSC Quantum 4 detector to a resolution of 2.8 Å. A series of 1 ̊ oscillation images were recorded with an exposure time of 10 seconds per image. More details are given with the scanned notes and the log file. </p>

opencc-by-4.0Nov 2016View details →
zenodo40/100

X-ray diffraction images for human native 5-aminolevulinic acid dehydratase (ALAD).

<p>X-ray diffraction images of human native ALAD collected at station 9.5 at synchrotron radiation source (SRS) Daresbury, UK, with a Marresearch 345 image plate detector on Sunday 26th April 1998. More details of the data collection are given in the files suffixed SUMMARY.</p>

opencc-by-4.0Nov 2016View details →
zenodo40/100

Original X-ray diffraction images for 5-aminolevulinic acid dehydratase (ALAD) from E. coli complexed with porphobilinogen.

<p>The diffraction images which allowed the original 2.1 Angstrom resolution structure determination of <em>Escherichia coli</em> ALAD co-crystallised with a non-covalently bound moiety of the product, porphobilinogen (PBG), are presented. </p>

opencc-by-4.0Nov 2016View details →
zenodo40/100

Atomic resolution X-ray diffraction images for methanol dehydrogenase from Methylobacterium extorquens.

<p>Atomic resolution X-ray diffraction images for methanol dehydrogenase from <em>Methylobacterium extorquens</em> collected at ESRF (Grenoble, France) using beamline ID29 in May 2002 with an ADSC detector. The diffraction resolution for the first pass is approximately 1.1 - 1.2 Angstroms and a second pass was collected to recoup the reflections that were overloaded in the first pass. More details of the data collection are in the included scanned notes and log files. </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

X-ray diffraction images for cytochrome cL from the methylotrophic bacterium Methylobacterium extorquens.

<p>X-ray diffraction images for cytochrome c<sub>L</sub> from <em>Methylobacterium extorquens</em> collected at the ESRF beamline ID14-2 using an ADSC detector in Feb 2001. The diffraction data extend to around 2.0 Angstroms resolution and were used for the initial structure determination of this protein. Further details in the log files and the notes.  </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

Atomic resolution X-ray diffraction images of native endothiapepsin.

<p>X-ray diffraction images that were collected at DESY (Hamburg) to a resolution of 0.9 Angstroms from native endothiapepsin. The data were collected using a MAR345 detector at beamline BW7B in June 1999. More details are in the included notes. </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

Atomic resolution X-ray diffraction images for endothiapepsin complexed with the inhibitor H261.

<p>X-ray diffraction images for a complex of endothiapepsin with the hydroxyethylene renin inhibitor H261 which were collected at DESY (Hamburg) in June 1998 using the beamline BW7B with a Mar image plate detector in two passes. The data extend to a resolution of almost 1.1 Angstroms. More details are given in the accompanying notes. </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

X-ray diffraction images for 5-aminolevulinic acid dehydratase with a putative reaction intermediate resembling the product porphobilinogen bound.

<p>X-ray diffraction images for yeast 5-aminolevulinic acid dehydratase co-crystallised with the substrate 5-aminolevulinic acid. The structure demonstrated a putative product-like intermediate bound covalently to Lys 263 with an amino side chain ligated to the active-site zinc ion in a position normally occupied by a catalytic hydroxide ion. The data were collected in two passes using the ESRF beamline ID29 in Feb 2002 and extend to approximately 1.6 Å resolution. </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

X-ray diffraction images for yeast 5-aminolevulinic acid dehydratase complexed with 4-oxosebacic acid.

<p>X-ray diffraction images for yeast 5-aminolaevulinic acid dehydratase complexed with 4-oxosebacic acid which were collected using beamline ID14-2 at the ESRF (Grenoble) in Feb 2001. </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

X-ray diffraction images for the H145E mutant of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis.

<p>X-ray diffraction images of the H145E mutant (prefixed h145e) which were collected in October 1995 using a graphite-monochromated copper K-alpha rotating anode source (wavelength 1.5418 Å) with a Marresearch 90 cm image plate detector at a distance of 120 mm from the crystal. The data were collected at room temperature in two passes, each consisting of 100 one degree rotations of the crystal. Each image had an exposure time of 20 minutes. The crystal was rotated in the capillary tube prior to collection of the second pass in order to record the 'blind' region of the diffraction pattern and this set of images is prefixed h145eb. </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

X-ray diffraction images for the H145Q mutant of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis.

<p>X-ray diffraction images collected from one crystal at room temperature using a rotating anode copper source (wavelength 1.5418 Å) and a 30 cm Marresearch image plate detector. The crystal-to-detector distance was 150 mm and a 90 mm image plate scan radius was used. Each of the 60 images had an exposure time of 20 minutes and corresponds to a 3 degree phi-rotation of the crystal. Diffraction extends to about 3.3 Å resolution. </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

X-ray diffraction images for bovine inositol monophosphatase.

<p>X-ray diffraction images for bovine inositol monophosphatase which were collected using the ESRF beamline ID14-4 to a resolution of around 1.4 Å. The data were collected in two passes, the second for measuring intensities that were overloaded in the first. More details are given in the included notes. </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

X-ray diffraction images for 5-aminolevulinic acid dehydratase (ALAD) from E. coli.

<p>X-ray diffraction images for <em>Escherichia coli</em> 5-aminolevulinic acid dehydratase (ALAD) which was crystallised in the presence of the inhibitor levulinic acid (15 mM) and bismuth nitrate (1 mM). The data were collected at beamline 9.6 at the SRS Daresbury Laboratory (UK) on 10th March 1994 using a 30 cm Marresearch image plate detector, a crystal temperature of 100 K, a wavelength of 0.88 Å and a crystal-to-detector distance was 300 mm. The oscillation angle was 2.5 degrees and 21 images were collected at constant dose in the time available. A wax image for determining the direct beam position was taken with the detector at a distance of 400 mm.</p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

X-ray diffraction images for yeast 5-aminolevulinic acid dehydratase complexed with 4-keto-5-aminohexanoic acid.

<p>X-ray diffraction images which were collected at the EMBL beamline BW7B, DESY (Hamburg) on 28th June 1999 using a Marresearch 345 image plate detector. The data were collected in three passes, images in the first main one having file prefix hykah, the second being a low-resolution run (lr) and, the last, a very high resolution (vhr) pass. More details are given in the notebook pages. </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

X-ray diffraction images for yeast 5-aminolevulinic acid dehydratase complexed with succinylacetone.

<p>X-ray diffraction images which were collected on 28th March 1999 at the EMBL beamline BW7B at DESY (Hamburg) using a Marresearch 345 image plate detector. More information in the notes. </p>

opencc-by-4.0Dec 2016View details →
zenodo40/100

X-ray diffraction images of yeast 5-aminolevulinic acid dehydratase complexed with substrate 5-aminolevulinic acid.

<p>X-ray diffraction images collected at the BW7B beamline at DESY (Hamburg) on 2 Jun 1998. More details in the notes. </p>

opencc-by-4.0Jan 2017View details →

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