Ultra-high Resolution Protein Crystallography

DOI Web Site 30 References

Bibliographic Information

Other Title
  • 構造生物学研究の新展開　　１．タンパク質構造研究に対する結晶学の役割　　タンパク質における超高分解能Ｘ線結晶構造解析
  • タンパク質における超高分解能X線結晶構造解析
  • タンパクシツ ニ オケル チョウ コウ ブンカイノウ Xセン ケッショウ コウゾウ カイセキ

Search this article

Abstract

Many protein structures have been determined by X-ray crystallography and deposited with the Protein Data Bank. However, these structures at usual resolution (1.5<d<3.0 Å) are insufficient in their precision and quantity for elucidating the molecular mechanism of protein functions directly from structural information. Several studies at ultra-high resolution (d<0.8 Å) have been performed with synchrotron radiation in the last decade. The highest resolution of the protein crystals was achieved at 0.54 Å resolution for a small protein, crambin. In such high resolution crystals, almost all of hydrogen atoms of proteins and some hydrogen atoms of bound water molecules are experimentally observed. In addition, outer-shell electrons of proteins can be analyzed by the multipole refinement procedure. However, the influence of X-rays should be precisely estimated in order to derive meaningful information from the crystallographic results. In this review, we summarize refinement procedures, current status and perspectives for ultra high resolution protein crystallography.

Journal

References(30)*help

See more

Related Projects

See more

Details 詳細情報について

Report a problem

Back to top