1B8Z
HU FROM THERMOTOGA MARITIMA
Summary for 1B8Z
Entry DOI | 10.2210/pdb1b8z/pdb |
Descriptor | PROTEIN (HISTONELIKE PROTEIN HU) (2 entities in total) |
Functional Keywords | thermotoga maritima, thermostable dna binding protein, dna binding protein |
Biological source | Thermotoga maritima |
Total number of polymer chains | 2 |
Total formula weight | 20036.20 |
Authors | Christodoulou, E.,Rypniewski, W.R.,Vorgias, C.E. (deposition date: 1999-02-03, release date: 2000-02-03, Last modification date: 2023-12-27) |
Primary citation | Christodoulou, E.,Vorgias, C.E. Cloning, overproduction, purification and crystallization of the DNA binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima. Acta Crystallogr.,Sect.D, 54:1043-1045, 1998 Cited by PubMed Abstract: The humar gene encoding for the histone-like DNA-binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima was efficiently overexpressed in Escherichia coli under the T7 promoter. The HU protein was purified using SP-Sepharose ion-exchange and heparin-affinity chromatography and was successfully crystallized in ammonium sulfate. The crystals were grown in the tetragonal form in space group P43 or P41 and have unit-cell dimensions a = b = 46.12, c = 77.56 A, alpha = beta = gamma = 90 degrees. The crystals diffract X-rays to 1.6 A resolution using synchrotron radiation and are suitable for determination of the HU structure at high resolution. PubMed: 9757133DOI: 10.1107/S0907444998000341 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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