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Crystallization, data collection and phasing of two digestive lysozymes from Musca domestica.


ABSTRACT: Lysozymes are mostly known for their defensive role against bacteria, but in several animals lysozymes have a digestive function. Here, the initial crystallographic characterization of two digestive lysozymes from Musca domestica are presented. The proteins were crystallized using the sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data were collected to a maximum resolution of 1.9 angstroms using synchrotron radiation. The lysozyme 1 and 2 crystals belong to the monoclinic space group P2(1) (unit-cell parameters a = 36.52, b = 79.44, c = 45.20 angstroms, beta = 102.97 degrees) and the orthorhombic space group P2(1)2(1)2 (unit-cell parameters a = 73.90, b = 96.40, c = 33.27 angstroms), respectively. The crystal structures were solved by molecular replacement and structure refinement is in progress.

SUBMITTER: Marana SR 

PROVIDER: S-EPMC2242927 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature

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Crystallization, data collection and phasing of two digestive lysozymes from Musca domestica.

Marana S R SR   Cançado F C FC   Valério A A AA   Ferreira C C   Terra W R WR   Barbosa J A R G JA  

Acta crystallographica. Section F, Structural biology and crystallization communications 20060724 Pt 8


Lysozymes are mostly known for their defensive role against bacteria, but in several animals lysozymes have a digestive function. Here, the initial crystallographic characterization of two digestive lysozymes from Musca domestica are presented. The proteins were crystallized using the sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data were collected to a maximum resolution of 1.9 angstroms using synchrotron radiat  ...[more]

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