Crystallization and preliminary X-ray analysis of the catalytic domain of endoglucanase from Clostridium cellulolyticum.
The catalytic domain of an endoglucanase belonging to family A (CelCCA) from an anaerobic bacterium (Clostridium cellulolyticum) has been crystallized in a form suitable for X-ray diffraction analysis. The crystals have been grown in the presence of polyethylene glycol 4000 using the vapour diffusion technique. The crystals, which diffract to 2.0 A resolution, belong to the orthorhombic space group P2(1)2(1)2(1) and have the following cell constants: a = 52.4 A, b = 76.2 A and c = 113.5 A.
Roig
V
V
Laboratoire de Cristallographie et Cristallisation des Macro-molécules Biologiques CNRS URA 1296, Université d'Aix-Marseille II, Faculté de Médecine Nord, France.
Fierobe
H P
HP
Ducros
V
V
Czjzek
M
M
Belaich
A
A
Gaudin
C
C
Belaich
J P
JP
Haser
R
R
D000595:Amino Acid Sequence; D002480:Cellulase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D003013:Clostridium / Q000201:enzymology*; D003460:Crystallization; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014961:X-Ray Diffraction / Q000379:methods
D002480:Cellulase