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Title
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Crystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei.
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Authors
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C.Divne,
I.Sinning,
J.Ståhlberg,
G.Pettersson,
M.Bailey,
M.Siika-aho,
E.Margolles-Clark,
T.Teeri,
T.A.Jones.
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Ref.
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J Mol Biol, 1993,
234,
905-907.
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PubMed id
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Abstract
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The catalytic core domains of cellobiohydrolase I (CBHI) and endoglucanase I
(EGI) from Trichoderma reesei have been crystallized using the hanging drop
vapour diffusion method. In the case of CBHI, use of polyethylene glycol 20,000,
and calcium chloride at low pH produced good quality single crystals suitable
for X-ray studies. The crystals belong to a primitive orthorhombic space group
with unit cell dimensions a = 84.0 A, b = 86.2 A, c = 111.8 A, and diffract
beyond 2.0 A resolution. Bipyramidal crystals of EGI core were grown from
ammonium sulphate at pH 7.5. The crystals are tetragonal, either P4(1)22 or the
enantiomorph P4(3)22, with cell dimensions a = b = 101.8 A and c = 198.0 A, and
at best diffract to a resolution of 2.5 A.
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