1Z0V

Crystal Structure of A. fulgidus Lon proteolytic domain

Summary for 1Z0V

• Entry DOI: 10.2210/pdb1z0v/pdb
• Related: 1Z0B 1Z0C 1Z0E 1Z0G 1Z0T 1Z0W
• Descriptor: Putative protease La homolog type (2 entities in total)
• Functional Keywords: atp-dependent protease, catalytic ser-lys dyad, b-type lon, hydrolase
• Biological source: Archaeoglobus fulgidus
• Cellular location: Cell membrane ; Multi-pass membrane protein : O29883
• Total number of polymer chains: 6
• Total formula weight: 131041.33

Authors

Dauter, Z.,Botos, I.,LaRonde-LeBlanc, N.,Wlodawer, A. (deposition date: 2005-03-02, release date: 2005-08-02, Last modification date: 2024-02-14)

Primary citation

Dauter, Z.,Botos, I.,LaRonde-LeBlanc, N.,Wlodawer, A.
Pathological crystallography: case studies of several unusual macromolecular crystals.
Acta Crystallogr.,Sect.D, 61:967-975, 2005

PubMed Abstract: Although macromolecular crystallography is rapidly becoming largely routine owing to advances in methods of data collection, structure solution and refinement, difficult cases are still common. To remind structural biologists about the kinds of crystallographic difficulties that might be encountered, case studies of several successfully completed structure determinations that utilized less than perfect crystals are discussed here. The structure of the proteolytic domain of Archaeoglobus fulgidus Lon was solved with crystals that contained superimposed orthorhombic and monoclinic lattices, a case not previously described for proteins. Another hexagonal crystal form of this protein exhibited an unusually high degree of non-isomorphism. Crystals of A. fulgidus Rio1 kinase exhibited both pseudosymmetry and twinning. Ways of identifying the observed phenomena and approaches to solving and refining macromolecular structures when only less than perfect crystals are available are discussed here.

PubMed: 15983420
DOI: 10.1107/S0907444905011285

Experimental method

X-RAY DIFFRACTION (3 Å)