Purification, crystallization, and preliminary X-ray analysis of human histidine decarboxylase
Purification, crystallization, and preliminary X-ray analysis of human histidine decarboxylase
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人组氨酸脱羧酶的纯化、结晶和初步 X 射线分析
DOI：
10.1107/s1744309112015692
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
Komori Hirofumi
中科院分区：
文献类型：
--
作者：
Komori Hirofumi
纯化了人组氨酸脱羧酶突变体的核心区，并与抑制剂L-组氨酸甲酯共结晶。使用同步辐射，从单晶中收集了分辨率为100 K到1.8 ä的数据集。该晶体属于C2空间群，晶胞参数a=215.16，b=112.72，c=171.39 ä，β=110.3°。以芳香族L氨基酸脱羧酶的结构为搜索模型，进行了分子置换。该晶体每个不对称单元含有三个二聚体，马修斯系数(Vm)为3.01 ä3 Da−1，溶剂含量估计为59.1%。
The core domain of a human histidine decarboxylase mutant was purified and cocrystallized with the inhibitor l-histidine methyl ester. Using synchrotron radiation, a data set was collected from a single crystal at 100 K to 1.8 Å resolution. The crystal belonged to space group C2, with unit-cell parameters a = 215.16, b = 112.72, c = 171.39 Å, β = 110.3°. Molecular replacement was carried out using the structure of aromatic l-amino-acid decarboxylase as a search model. The crystal contained three dimers per asymmetric unit, with a Matthews coefficient (VM) of 3.01 Å3 Da−1 and an estimated solvent content of 59.1%.