Preliminary analysis of crystals of 4-oxalocrotonate tautomerase, an enzyme composed of unusually small monomers.

Preliminary analysis of crystals of 4-oxalocrotonate tautomerase, an enzyme composed of unusually small monomers.
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4-草酰巴豆酸互变异构酶晶体的初步分析,这是一种由异常小的单体组成的酶。

DOI:
10.1006/jmbi.1993.1300
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发表时间:
1993
影响因子:
5.6
通讯作者:
Whitman,CP
Whitman,CP
中科院分区:
生物学2区
文献类型:
--
作者:
Davenport,RC;Whitman,CP

文献摘要

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Crystals of 4-oxalocrotonate tautomerase have been obtained by the vapor-diffusion method using polyethylene glycol as precipitant. The crystals belong to the orthorhombic space groupP212121, with unit cell parametersa= 118·1,b= 95·6,c= 97·4, α = β = γ = 90° and diffract well to at least 2·7 Å resolution. There are approximately ten 6811 dalton subunits of the enzyme per asymmetric unit, giving a crystal solvent content of 70%.