Trigonal catalase crystals: a new molecular packing assignment obtained from sections preserved with tannic acid.
The molecular packing of a trigonal crystal form of catalase initially studied by Longley [1] has been re-evaluated. Sections of crystals fixed and preserved with tannic acid were obtained parallel to the (001) and (100) planes. Specimens prepared by either conventional or low temperature embedding maintained 20 A resolution after sectioning. The space group of the crystals is either P3(1)21 or P3(2)21 and the observed unit cell parameters for (001) and (100) are a = b = 174 A, gamma = 119 degrees and b = 189 A, c = 248 A with alpha = 89.5 degrees. Computer-based reconstructions of two principal projections coupled with crystal density measurements allowed the deduction that there is one catalase tetramer per asymmetric unit. The crystal structure consists of 6 molecules packed closely about a common triad screw axis. This interpretation differs from that proposed by Longley [J. Mol. Biol. 30 (1967) 323], because thin sections of embedded crystals were assumed a priori to be positively stained in the early work; in actuality the sections were negatively stained. We also demonstrate that tannic acid fixation can lead to well preserved, positively stained crystal sections under certain conditions.
D000818:Animals; D002374:Catalase; D002417:Cattle; D003461:Crystallography / Q000379:methods; D005404:Fixatives; D005615:Freezing; D047348:Hydrolyzable Tannins; D008099:Liver / Q000201:enzymology; D011487:Protein Conformation
D005404:Fixatives; D047348:Hydrolyzable Tannins; D002374:Catalase