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Title
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The crystal structure of beta-lactamase from Staphylococcus aureus at 0.5 nm resolution.
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Authors
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J.Moult,
L.Sawyer,
O.Herzberg,
C.L.Jones,
A.F.Coulson,
D.W.Green,
M.M.Harding,
R.P.Ambler.
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Ref.
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Biochem J, 1985,
225,
167-176.
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PubMed id
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Abstract
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The preparation, crystallization and low-resolution structure determination of
beta-lactamase (EC 3.5.2.6, 'penicillinase') from Staphylococcus aureus is
described. The enzyme crystallizes in space group I222 with 1 molecule per
asymmetric unit and cell dimensions a = 5.45(1), b = 9.39(1) and c = 13.87(2)
nm. The structure was determined at 0.5 nm resolution by using phases calculated
from (NH4)2Pt(CN)4 and KAu(CN)2 derivatives. The mean figure of merit mean value
of m, for the 1106 reflexions used was 0.70. Difference Fourier syntheses for
data collected from crystals soaked in platinum D-methionine and in
6-(4-hydroxy-3,5-di-iodobenzamido)penicilloic acid revealed the likely position
of the active site of the enzyme.
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