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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.
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Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.

机译：奇异果甜蛋白在六角结构空间群:包装比较联系人在四个晶体晶格。

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摘要

The intensely sweet protein thaumatin has been crystallized in a hexagonal lattice after a temperature shift from 293 to 277 K. The structure of the protein in the new crystal was solved at 1.6 A resolution. The protein fold is identical to that found in three other crystal forms grown in the presence of crystallizing agents of differing chemical natures. The proportions of lattice interactions involving hydrogen bonds, hydrophobic or ionic groups differ greatly from one form to another. Moreover, the distribution of acidic and basic residues taking part in contacts also varies. The hexagonal packing is characterized by the presence of channels parallel to the c axis that are so wide that protein molecules can diffuse through them.
机译：强烈的甜蛋白奇异果甜蛋白在六角形晶格后结晶从293年到277 K温度转变。在新晶体结构的蛋白质1.6决议来解决。相同的发现在其他三个晶体生长在结晶的存在形式代理不同的化学性质。比例的晶格相互作用涉及氢键,疏水或离子组有很大的不同从一种形式到另一个地方。此外,酸性和碱性的分布残基参与接触也各不相同。六角包装的特点是频道c轴平行太宽,蛋白质分子扩散吗通过他们。

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