Crystallization and preliminary X-ray analysis of human carbonic anhydrase III

David M. Duda, Craig Yoshioka, Lakshmanan Govindasamy, Haiqian An, Chingkuang Tu, David N. Silverman, Robert McKenna

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Carbonic anhydrases catalyze the interconversion of carbon dioxide to bicarbonate. Human carbonic anhydrase isozyme III with a C-terminal hexahistidine tag was overexpressed in Eschericha coli, purified and crystallized. Diffraction data (93.4% completeness) were collected to 2.2 Å resolution on an in-house R-AXIS IV++ image-plate system with Osmic mirrors and a Rigaku HU-H3R CU rotating-anode generator operating at 50 kV and 100 mA. A 60° sweep of data were collected from a single crystal with a crystal-to-detector distance of 150 mm and a 0.5° oscillation angle per frame using an exposure of 60 s per frame at 293 K. The crystals were shown to conform to the Laue hexagonal crystal system P6, with unit-cell parameters a = 44.7, c = 222.5 Å and a scaling Rsym of 0.087 for 11 962 unique reflections. Using the known crystal structure of the rat form of carbonic anhydrase isozyme III, a molecular-replacement model was built. This model was used for rotation and translation searches and uniquely defined the space group as P65. Rigid-body refinement of the model was used to generate an initial phased electron-density map with an Rwork of 31.17%.

Original languageEnglish (US)
Pages (from-to)849-852
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Issue number5
StatePublished - 2002

ASJC Scopus subject areas

  • Structural Biology


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