The MORPHEUS II protein crystallization screen
Abstract
MORPHEUS II is a 96-condition initial crystallization screen formulated de novo. The screen incorporates reagents selected from the Protein Data Bank to yield crystals that are not observed in traditional conditions. In addition, the formulation facilitates the optimization and cryoprotection of crystals. High-quality macromolecular crystals are a prerequisite for the process of protein structure determination by X-ray diffraction. Unfortunately, the relative yield of diffraction-quality crystals from crystallization experiments is often very low. In this context, innovative crystallization screen formulations are continuously being developed. In the past, MORPHEUS, a screen in which each condition integrates a mix of additives selected from the Protein Data Bank, a cryoprotectant and a buffer system, was developed. Here, MORPHEUS II, a follow-up to the original 96-condition initial screen, is described. Reagents were selected to yield crystals when none might be observed in traditional initial screens. Besides, the screen includes heavy atoms for experimental phasing and small polyols to ensure the cryoprotection of crystals. The suitability of the resulting novel conditions is shown by the crystallization of a broad variety of protein samples and their efficiency is compared with commercially available conditions.
- Authors:
-
- MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH (United Kingdom)
- Publication Date:
- OSTI Identifier:
- 22389082
- Resource Type:
- Journal Article
- Journal Name:
- Acta crystallographica. Section F, Structural biology communications
- Additional Journal Information:
- Journal Volume: 71; Journal Issue: Pt 7; Other Information: PMCID: PMC4498703; PMID: 26144227; PUBLISHER-ID: en5565; PUBLISHER-ID: S2053230X1500967X; OAI: oai:pubmedcentral.nih.gov:4498703; Copyright (c) Gorrec 2015; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 2053-230X
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ATOMS; BUFFERS; CRYSTALLIZATION; CRYSTALS; EFFICIENCY; OPTIMIZATION; PROTEIN STRUCTURE; PROTEINS; X-RAY DIFFRACTION; YIELDS
Citation Formats
Gorrec, Fabrice. The MORPHEUS II protein crystallization screen. United States: N. p., 2015.
Web. doi:10.1107/S2053230X1500967X.
Gorrec, Fabrice. The MORPHEUS II protein crystallization screen. United States. https://doi.org/10.1107/S2053230X1500967X
Gorrec, Fabrice. 2015.
"The MORPHEUS II protein crystallization screen". United States. https://doi.org/10.1107/S2053230X1500967X.
@article{osti_22389082,
title = {The MORPHEUS II protein crystallization screen},
author = {Gorrec, Fabrice},
abstractNote = {MORPHEUS II is a 96-condition initial crystallization screen formulated de novo. The screen incorporates reagents selected from the Protein Data Bank to yield crystals that are not observed in traditional conditions. In addition, the formulation facilitates the optimization and cryoprotection of crystals. High-quality macromolecular crystals are a prerequisite for the process of protein structure determination by X-ray diffraction. Unfortunately, the relative yield of diffraction-quality crystals from crystallization experiments is often very low. In this context, innovative crystallization screen formulations are continuously being developed. In the past, MORPHEUS, a screen in which each condition integrates a mix of additives selected from the Protein Data Bank, a cryoprotectant and a buffer system, was developed. Here, MORPHEUS II, a follow-up to the original 96-condition initial screen, is described. Reagents were selected to yield crystals when none might be observed in traditional initial screens. Besides, the screen includes heavy atoms for experimental phasing and small polyols to ensure the cryoprotection of crystals. The suitability of the resulting novel conditions is shown by the crystallization of a broad variety of protein samples and their efficiency is compared with commercially available conditions.},
doi = {10.1107/S2053230X1500967X},
url = {https://www.osti.gov/biblio/22389082},
journal = {Acta crystallographica. Section F, Structural biology communications},
issn = {2053-230X},
number = Pt 7,
volume = 71,
place = {United States},
year = {Sat Jun 27 00:00:00 EDT 2015},
month = {Sat Jun 27 00:00:00 EDT 2015}
}