Crystallization, data collection and phasing of two digestive lysozymes from Musca domestica.
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.
Marana
S R
SR
Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil.
Cançado
F C
FC
Valério
A A
AA
Ferreira
C
C
Terra
W R
WR
Barbosa
J A R G
JA
D000818:Animals; D003460:Crystallization; D004064:Digestive System / Q000201:enzymology; D006793:Houseflies / Q000201:enzymology*; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification; D009113:Muramidase / Q000737:chemistry* / Q000302:isolation & purification; D017356:Synchrotrons; D014961:X-Ray Diffraction
D007527:Isoenzymes; D009113:Muramidase