title: Growth of protein crystals in hydrogels prevents osmotic shock.
abstract: High-throughput protein X-ray crystallography offers a significant opportunity to facilitate drug discovery. The most reliable approach is to determine the three-dimensional structure of the protein-ligand complex by soaking the ligand in apo crystals. However, protein apo crystals produced by conventional crystallization in a solution are fatally damaged by osmotic shock during soaking. To overcome this difficulty, we present a novel technique for growing protein crystals in a high-concentration hydrogel that is completely gellified and exhibits high strength. This technique allowed us essentially to increase the mechanical stability of the crystals, preventing serious damage to the crystals caused by osmotic shock. Thus, this method may accelerate structure-based drug discoveries.
authors.affiliation: Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan. sugiyama@chem.eng.osaka-u.ac.jp
authors.forename: Shigeru
authors.initials: S
authors.lastname: Sugiyama
authors.forename: Mihoko
authors.initials: M
authors.lastname: Maruyama
authors.forename: Gen
authors.initials: G
authors.lastname: Sazaki
authors.forename: Mika
authors.initials: M
authors.lastname: Hirose
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Adachi
authors.forename: Kazufumi
authors.initials: K
authors.lastname: Takano
authors.forename: Satoshi
authors.initials: S
authors.lastname: Murakami
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Inoue
authors.forename: Yusuke
authors.initials: Y
authors.lastname: Mori
authors.forename: Hiroyoshi
authors.initials: H
authors.lastname: Matsumura
mesh_terms: D001696:Biomechanical Phenomena; D003460:Crystallization / Q000379:methods*; D006244:Hardness; D020100:Hydrogels / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D009997:Osmotic Pressure; D055550:Protein Stability
chemical_list: D020100:Hydrogels; D009113:Muramidase