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5AVN

The 1.03 angstrom structure (P212121) of glucose isomerase crystallized in high-strength agarose hydrogel

Summary for 5AVN
Entry DOI10.2210/pdb5avn/pdb
Related5AVD 5AVG 5AVH
DescriptorXylose isomerase, MANGANESE (II) ION, CALCIUM ION, ... (5 entities in total)
Functional Keywordsxylose isomerase, hydrogel, isomerase
Biological sourceStreptomyces rubiginosus
Total number of polymer chains2
Total formula weight86878.49
Authors
Sugiyama, S.,Shimizu, N.,Maruyama, N.,Sazaki, G.,Adachi, H.,Takano, K.,Murakami, S.,Inoue, T.,Mori, Y.,Matsumura, H. (deposition date: 2015-06-23, release date: 2015-07-08, Last modification date: 2023-11-08)
Primary citationSugiyama, S.,Maruyama, M.,Sazaki, G.,Hirose, M.,Adachi, H.,Takano, K.,Murakami, S.,Inoue, T.,Mori, Y.,Matsumura, H.
Growth of protein crystals in hydrogels prevents osmotic shock
J.Am.Chem.Soc., 134:5786-5789, 2012
Cited by
PubMed 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.
PubMed: 22435400
DOI: 10.1021/ja301584y
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.03 Å)
Structure validation

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