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Crystallization and preliminary X-ray crystallographic analysis of the protease inhibitor ecotin.
J Mol Biol. 1993 Feb 20; 229(4):1157-8.JM

Abstract

Ecotin, a novel serine protease inhibitor isolated from Escherichia coli, has been crystallized using polyethylene glycol 1500 as the precipitating agent. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters of a = 39.22 A, b = 84.86 A, and c = 98.74 A. The asymmetric unit contains one dimeric molecule of ecotin, with a crystal volume per protein mass (Vm) of 2.55 A3/Da and a solvent content of 51.8% by volume. The crystals diffract to at least 2.2 A using a conventional X-ray source, and X-ray data have been collected to 2.7 A Bragg spacing from a native crystal.

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Authors+Show Affiliations

Shin DH
Department of Chemistry, College of Natural Sciences, Seoul National University, Korea.
Hwang KY
No affiliation info available
Kim KK
No affiliation info available
Lee HR
No affiliation info available
Lee CS
No affiliation info available
Chung CH
No affiliation info available
Suh SW
No affiliation info available

MeSH

Bacterial ProteinsCrystallizationEscherichia coliEscherichia coli ProteinsPeriplasmic ProteinsProtease InhibitorsX-Ray Diffraction

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8445642

Citation

Shin, D H., et al. "Crystallization and Preliminary X-ray Crystallographic Analysis of the Protease Inhibitor Ecotin." Journal of Molecular Biology, vol. 229, no. 4, 1993, pp. 1157-8.
Shin DH, Hwang KY, Kim KK, et al. Crystallization and preliminary X-ray crystallographic analysis of the protease inhibitor ecotin. J Mol Biol. 1993;229(4):1157-8.
Shin, D. H., Hwang, K. Y., Kim, K. K., Lee, H. R., Lee, C. S., Chung, C. H., & Suh, S. W. (1993). Crystallization and preliminary X-ray crystallographic analysis of the protease inhibitor ecotin. Journal of Molecular Biology, 229(4), 1157-8.
Shin DH, et al. Crystallization and Preliminary X-ray Crystallographic Analysis of the Protease Inhibitor Ecotin. J Mol Biol. 1993 Feb 20;229(4):1157-8. PubMed PMID: 8445642.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray crystallographic analysis of the protease inhibitor ecotin. AU - Shin,D H, AU - Hwang,K Y, AU - Kim,K K, AU - Lee,H R, AU - Lee,C S, AU - Chung,C H, AU - Suh,S W, PY - 1993/2/20/pubmed PY - 1993/2/20/medline PY - 1993/2/20/entrez SP - 1157 EP - 8 JF - Journal of molecular biology JO - J Mol Biol VL - 229 IS - 4 N2 - Ecotin, a novel serine protease inhibitor isolated from Escherichia coli, has been crystallized using polyethylene glycol 1500 as the precipitating agent. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters of a = 39.22 A, b = 84.86 A, and c = 98.74 A. The asymmetric unit contains one dimeric molecule of ecotin, with a crystal volume per protein mass (Vm) of 2.55 A3/Da and a solvent content of 51.8% by volume. The crystals diffract to at least 2.2 A using a conventional X-ray source, and X-ray data have been collected to 2.7 A Bragg spacing from a native crystal. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/8445642/Crystallization_and_preliminary_X_ray_crystallographic_analysis_of_the_protease_inhibitor_ecotin_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(83)71112-5 DB - PRIME DP - Unbound Medicine ER -