ArticleActa crystallographica. Section F, Structural biology communications2015
The MORPHEUS II protein crystallization screen.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
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- Discovery and binding mode of small molecule inhibitors of the apo form of human TDO2.Scientific reports · 2024Article
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- Diversity of mechanisms to control bacterial GTP homeostasis by the mutually exclusive binding of adenine and guanine nucleotides to IMP dehydrogenase.Protein science : a publication of the Protein Society · 2022Article
- The FUSION protein crystallization screen.Journal of applied crystallography · 2022Article
- Structure of the decoy module of human glycoprotein 2 and uromodulin and its interaction with bacterial adhesin FimH.Nature structural & molecular biology · 2022Article
- Crystal structure and functional analysis of mycobacterial erythromycin resistance methyltransferase Erm38 reveals its RNA-binding site.The Journal of biological chemistry · 2022Article
- Crystal structure of betaine aldehyde dehydrogenase from Burkholderia pseudomallei.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Crystal polymorphism in fragment-based lead discovery of ligands of the catalytic domain of UGGT, the glycoprotein folding quality control checkpoint.Frontiers in molecular biosciences · 2022Article
- Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase.Structure (London, England : 1993) · 2021Article
- RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination.Nature communications · 2021Article
- C-phycocyanin as a highly attractive model system in protein crystallography: unique crystallization properties and packing-diversity screening.Acta crystallographica. Section D, Structural biology · 2021Article
- A molecular basis for the T cell response in HLA-DQ2.2 mediated celiac disease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Partial catalytic Cys oxidation of human GAPDH to Cys-sulfonic acid.Wellcome open research · 2020Article
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Abstract
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.
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