1YYF
Correction of X-ray Intensities from an HslV-HslU co-crystal containing lattice translocation defects
Summary for 1YYF
Entry DOI | 10.2210/pdb1yyf/pdb |
Descriptor | ATP-dependent hsl protease ATP-binding subunit hslU, ATP-dependent protease hslV, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
Functional Keywords | lattice translocation defect, hslv-hslu, atp-dependent proteolysis, quaternary structure, chaperone-hydrolase complex, chaperone/hydrolase |
Biological source | Escherichia coli More |
Cellular location | Cytoplasm: P0A6H5 Cytoplasm (By similarity): P39070 |
Total number of polymer chains | 4 |
Total formula weight | 139180.47 |
Authors | Wang, J.,Rho, S.H.,Park, H.H.,Eom, S.H. (deposition date: 2005-02-24, release date: 2005-07-12, Last modification date: 2024-02-14) |
Primary citation | Wang, J.,Rho, S.H.,Park, H.H.,Eom, S.H. Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects. Acta Crystallogr.,Sect.D, 61:932-941, 2005 Cited by PubMed Abstract: Because of lattice-translocation defects, two identical but translated lattices can coexist as a single coherent mosaic block in a crystal. The observed structure in such cases is a weighted sum of two identical but translated structures, one from each lattice; the observed structure factors are a weighted vector sum of the structure factors with identical unit amplitudes but shifted phases. The correction of X-ray intensities from a single crystal containing these defects of the hybrid HslV-HslU complex, which consists of Escherichia coli HslU and Bacillus subtilis HslV (also known as CodW), is reported. When intensities are not corrected, a biologically irrelevant complex (with CodW from one lattice and HslU from another) is implied to exist. Only upon correction does a biologically functional CodW-HslU complex structure emerge. PubMed: 15983416DOI: 10.1107/S0907444905009546 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (4.16 Å) |
Structure validation
Download full validation report
