Special Issue "Protein Crystallography 2016"

A special issue of Biomolecules (ISSN 2218-273X).

Deadline for manuscript submissions: closed (30 June 2017)

Special Issue Editor

Guest Editor
Prof. Dr. Dilano K. Saldin

Department of Physics, University of Wisconsin Milwaukee, Milwaukee, WI, USA
Website | E-Mail
Interests: XFEL, membrane protein structure, weak signals, unknown orientations

Special Issue Information

Dear Colleagues,

We are interested in the use of radiation from the X-ray free electron laser (XFEL) for protein structure determination. An XFEL is capable of producing X-rays that are ten billion (1010) times brighter that any previous X-ray source. When one considers that protein crystallography is usually done on samples containing perhaps a trillion (1012) molecules, an intriguing question is whether the extra brightness of the XFEL will allow structure determination from individual molecules. One has to be content with signals, which are perhaps a hundred times smaller. Of course, a single molecule will scatter only diffuse intensities, devoid of Bragg spots. Finally, sample delivery systems probably will not be able to control the orientations of the samples, which should perhaps be regarded as randomly oriented.

Despite these differences with traditional protein crystallography, if structure determination is possible, it would allow structure determination of even uncrystallized proteins. This is important because there exist entire classes of proteins, e.g., membrane proteins, which are very resistant to crystallization.

Prof. Dr. Dilano K. Saldin
Guest Editors

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Keywords

  • XFEL
  • membrane protein structure
  • weak signals
  • unknown orientations

Published Papers (1 paper)

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Review

Open AccessReview In Quest for Improved Drugs against Diabetes: The Added Value of X-ray Powder Diffraction Methods
Biomolecules 2017, 7(3), 63; doi:10.3390/biom7030063
Received: 10 July 2017 / Revised: 14 August 2017 / Accepted: 16 August 2017 / Published: 22 August 2017
PDF Full-text (6023 KB) | HTML Full-text | XML Full-text
Abstract
Human insulin (HI) is a well-characterized natural hormone which regulates glycose levels into the blood-stream and is widely used for diabetes treatment. Numerous studies have manifested that despite significant efforts devoted to structural characterization of this molecule and its complexes with organic compounds
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Human insulin (HI) is a well-characterized natural hormone which regulates glycose levels into the blood-stream and is widely used for diabetes treatment. Numerous studies have manifested that despite significant efforts devoted to structural characterization of this molecule and its complexes with organic compounds (ligands), there is still a rich diagram of phase transitions and novel crystalline forms to be discovered. Towards the improvement of drug delivery, identification of new insulin polymorphs from polycrystalline samples, simulating the commercially available drugs, is feasible today via macromolecular X-ray powder diffraction (XRPD). This approach has been developed, and is considered as a respectable method, which can be employed in biosciences for various purposes, such as observing phase transitions and characterizing bulk pharmaceuticals. An overview of the structural studies on human insulin complexes performed over the past decade employing both synchrotron and laboratory sources for XRPD measurements, is reported herein. This review aims to assemble all of the recent advances in the diabetes treatment field in terms of drug formulation, verifying in parallel the efficiency and applicability of protein XRPD for quick and accurate preliminary structural characterization in the large scale. Full article
(This article belongs to the Special Issue Protein Crystallography 2016)
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