ArticleActa crystallographica. Section F, Structural biology communications2015
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein from Spiroplasma melliferum KC3.
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 8 papers.
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Who cites it
8 citing papers in PubMed, 26 citations in OpenAlex.
- From Structure to Function: Analysis of the First Monomeric Pyridoxal-5'-Phosphate-Dependent Transaminase from the BacteriumBiomolecules · 2024Article
- Expanded Substrate Specificity in D-Amino Acid Transaminases: A Case Study of Transaminase fromInternational journal of molecular sciences · 2023Article
- To the Understanding of Catalysis by D-Amino Acid Transaminases: A Case Study of the Enzyme fromMolecules (Basel, Switzerland) · 2023Article
- The Uncommon Active Site of D-Amino Acid Transaminase fromMolecules (Basel, Switzerland) · 2021Article
- Consensus protein engineering on the thermostable histone-like bacterial protein HUs significantly improves stability and DNA binding affinity.Extremophiles : life under extreme conditions · 2020Article
- Comparison of histone-like HU protein DNA-binding properties and HU/IHF protein sequence alignment.PloS one · 2017Article
- Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3.Scientific reports · 2016Article
- HU histone-like DNA-binding protein from Thermus thermophilus: structural and evolutionary analyses.Extremophiles : life under extreme conditions · 2016Article
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Authors and funding
8 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
HU proteins belong to the nucleoid-associated proteins (NAPs) that are involved in vital processes such as DNA compaction and reparation, gene transcription etc. No data are available on the structures of HU proteins from mycoplasmas. To this end, the HU protein from the parasitic mycoplasma Spiroplasma melliferum KC3 was cloned, overexpressed in Escherichia coli and purified to homogeneity. Prismatic crystals of the protein were obtained by the vapour-diffusion technique at 4°C. The crystals diffracted to 1.36 Å resolution (the best resolution ever obtained for a HU protein). The diffraction data were indexed in space group C2 and the structure of the protein was solved by the molecular-replacement method with one monomer per asymmetric unit.
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