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Title
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Crystallization of a genetically engineered water-soluble primary penicillin target enzyme. The high molecular mass PBP2x of Streptococcus pneumoniae.
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Authors
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P.Charlier,
G.Buisson,
O.Dideberg,
J.Wierenga,
W.Keck,
G.Laible,
R.Hakenbeck.
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Ref.
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J Mol Biol, 1993,
232,
1007-1009.
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PubMed id
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Abstract
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A genetically engineered water-soluble derivative of PBP2x of Streptococcus
pneumoniae has been produced, purified and crystallized in a form suitable for
X-ray diffraction analysis. The best crystals have been grown at 15 degrees C,
from solutions containing 8% polyethylene glycol 10,000 at pH values ranging
from 3.9 to 6.0. These crystals diffract to a resolution of 3.5 A and have a
space group P6(1)22 (or enantiomorph) with unit cell dimensions of a = b = 162.2
A, c = 171.8 A, alpha = beta = 90 degrees, gamma = 120 degrees. The molecular
mass and cell dimensions suggest that there is one molecule of enzyme per
asymmetric unit. The breakdown of a chromogenic cephalosporin derivative
diffused into a crystal reveals clearly that the enzyme is active in the
crystalline state.
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