Gerald Stubbs
Last active: 2/15/2016

Preliminary crystallographic examination of a novel fungal lysozyme from Chalaropsis.

Lyne JE, Carter DC, He XM, Stubbs G, Hash JH
J Biol Chem. 1990 265 (12): 6928-30

PMID: 2324106

The lysozyme from the fungus of the Chalaropsis species has been crystallized. This lysozyme (Mr 22,415) displays no sequence homology with avian, phage, or mammalian lysozymes, however, preliminary studies indicate significant sequence homology with the bacterial lysozyme from Streptomyces. Both enzymes are unusual in possessing beta-1,4-N-acetylmuramidase and beta-1,4-N,6-O-diacetylmuramidase activity. The crystals grow from solutions of ammonium sulfate during growth periods from several months to a year. The space group is P2(1)2(1)2(1) with a = 34.0 A, b = 42.6 A, c = 122.1 A. Preliminary data indicate that there is 1 molecule/asymmetric unit. A complete native data set has been collected to 2.57-A resolution. The crystals are highly ordered and exhibit diffraction patterns to d-spacings less than 1.5 A.

MeSH Terms (4)

Crystallization Mitosporic Fungi Muramidase X-Ray Diffraction

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