[19p-H112-1~15] 15.1 Bulk crystal growth

[19p-H112-4] Relaxation of a large amount of local strain in protein crystals by using seed crystals

〇Haruhiko Koizumi¹, Satishi Uda¹, Masaru Tachibana², Katsuo Tsukamoto³, Kenichi Kojima⁴, Jun Nozawa¹ (1.IMR, Tohoku Univ., 2.Yokohama City Univ., 3.Osaka Univ., 4.Yokohama Soei Univ.)

Keywords:Protein crystal,Rocking-curve measurements,Strain relaxation

In order to allow both structure-guided drug design and controlled drug delivery, it is important to determine the 3D structures of protein molecules. At present, these structures are primarily determined using X-ray diffraction analysis, and therefore high-quality single crystals of proteins are required, even though these are quite difficult to obtain. Previously, we have revealed that imperfections in protein crystals are predominantly caused by local strain and misorientation between subgrains. In this presentation, we try to release a large amount of local strain in protein crystals, by using seed crystals.