A preliminary study of space- and ground-grown insulin crystals by X-ray diffraction and by light scattering tomography

A preliminary study of space- and ground-grown insulin crystals by X-ray diffraction and by light scattering tomography

For the first time, both X-ray diffraction and light scattering tomography were used to study the same set of space- and ground-grown protein crystals. X-ray diffraction of the insulin crystals grown from T6 insulin solutions by temperature reduction showed that space-grown crystals diffract to high...

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Bibliographic Details
Published in:Journal of crystal growth Vol. 232; no. 1; pp. 511 - 519
Main Authors: De Mattei, R.C, Feigelson, R.S, Bray, T.L, DeLucas, L.J, Symersky, J
Format: Journal Article Conference Proceeding
Language:English
Published: Amsterdam Elsevier B.V 01-11-2001
Elsevier
Subjects:
Aminoacids, peptides. Hormones. Neuropeptides
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Crystal defects
Crystal growth
Deformation
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods
Light scattering
Molecular crystals
Proteins
Tomography
X ray diffraction analysis
Crystal growth
Earth
Protein hormone
Pancreatic hormone
Light scattering
Tomography
Biological macromolecule
Space shuttle
X ray diffraction
Insulin
Microgravity
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Summary:For the first time, both X-ray diffraction and light scattering tomography were used to study the same set of space- and ground-grown protein crystals. X-ray diffraction of the insulin crystals grown from T6 insulin solutions by temperature reduction showed that space-grown crystals diffract to higher resolution then those grown on the ground. The light scattering tomographs revealed that the space-grown crystals contained very few spherical micro-defects while the ground-grown ones had large numbers of extended micro-defects and dislocations. The tomographs also gave insight into the methods of defect formation. This study marks the beginning of qualification of light scattering tomograph as a tool for determining the suitability of a protein for use in X-ray diffraction studies.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:0022-0248
1873-5002
DOI:10.1016/S0022-0248(01)01159-9