X-ray crystallography is one of the main techniques currently available for solving atomic structures of macromolecules such as proteins and nucleic acids. Structure determination is a long and ...time-consuming process, and a complete understanding of the solved structure may take an even longer time. Final product of whole task will give us in-depth ideas of how macromolecules handle various tasks in the cell. Three chapters are concentrated on the description of structure determinations and analyses of four different macromolecules, GMH3, GMH4, cis-syn cyclobutane thymine dimer lesion containing DNA, and the heme domain of DOS protein. The last chapter reviews our model of calsequestrin polymerization. We proposed the model based on the previous crystal structure from rabbit skeletal calsequestrin solved by our group.
The heme‐containing PAS domain of the direct oxygen‐sensor protein (DOSH), a bona fide oxygen‐sensor protein, has been cloned from Escherichia coli strain K12 and successfully purified. The oxidized ...form of this protein was crystallized by the hanging‐drop method with a PEG 8000‐based precipitant. Preliminary X‐ray diffraction studies of the PAS‐domain crystal show that it belongs to the orthorhombic space group P212121, with unit‐cell parameters a = 46.1, b = 68.1, c = 82.6 Å. A complete diffraction data set was collected to 1.9 Å for MAD phasing. The electron‐density map shows two molecules in an asymmetric unit and a unique six‐coordination of the heme iron.
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