Development of an X-ray fluorescence holographic measurement system for protein crystals.
Development of an X-ray fluorescence holographic measurement system for protein crystals.
复制标题
开发蛋白质晶体的 X 射线荧光全息测量系统。
DOI:
10.1063/1.4953453
复制
发表时间:
2016
期刊:
影响因子:
--
通讯作者:
K. Hayashi
中科院分区:
文献类型:
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作者:
A. Sato‐Tomita;N. Shibayama;N. Happo;K. Kimura;Takahiro Okabe;T. Matsushita;Sam;Y. Sasaki;K. Hayashi
Experimental procedure and setup for obtaining X-ray fluorescence hologram of crystalline metalloprotein samples are described. Human hemoglobin, an α2β2 tetrameric metalloprotein containing the Fe(II) heme active-site in each chain, was chosen for this study because of its wealth of crystallographic data. A cold gas flow system was introduced to reduce X-ray radiation damage of protein crystals that are usually fragile and susceptible to damage. A χ-stage was installed to rotate the sample while avoiding intersection between the X-ray beam and the sample loop or holder, which is needed for supporting fragile protein crystals. Huge hemoglobin crystals (with a maximum size of 8 × 6 × 3 mm(3)) were prepared and used to keep the footprint of the incident X-ray beam smaller than the sample size during the entire course of the measurement with the incident angle of 0°-70°. Under these experimental and data acquisition conditions, we achieved the first observation of the X-ray fluorescence hologram pattern from the protein crystals with minimal radiation damage, opening up a new and potential method for investigating the stereochemistry of the metal active-sites in biomacromolecules.
DOI:
--
发表时间:
2019
期刊:
影响因子:
--
作者:
K. Kimura;T. Nishioka;Y. Yamamoto;K. Hagihara;H. Izumo;N. Happo;S. Hosokawa;E. Abe;M. Suzuki;T. Matsushita;and K. Hayashi
通讯作者:
and K. Hayashi