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Crystallization and preliminary X-ray diffraction analysis of the human dimeric S-Lac lectin (L-14-II).
J Mol Biol. 1993 Oct 05; 233(3):553-5.JM

Abstract

The human recombinant S-Lac lectin, L-14-II, produced in an Escherichia coli expression system, has been co-crystallized in the presence of lactose by the hanging drop vapor diffusion method. The crystals grow in space group P2(1)2(1)2(1) with unit cell dimensions of a = 43.6 A, b = 57.8 A, c = 108.2 A, with a dimer in the asymmetric unit. On a conventional rotating anode the crystals diffract to at least 2.8 A resolution.

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Authors+Show Affiliations

Lobsanov YD
Department of Molecular Genetics, University of Toronto, Ontario, Canada.
Gitt MA
No affiliation info available
Leffler H
No affiliation info available
Barondes S
No affiliation info available
Rini JM
No affiliation info available

MeSH

Crystallography, X-RayEscherichia coliGalectinsHemagglutininsHumansLectinsProtein ConformationRecombinant Proteins

Pub Type(s)

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

Language

eng

PubMed ID

8411163

Citation

Lobsanov, Y D., et al. "Crystallization and Preliminary X-ray Diffraction Analysis of the Human Dimeric S-Lac Lectin (L-14-II)." Journal of Molecular Biology, vol. 233, no. 3, 1993, pp. 553-5.
Lobsanov YD, Gitt MA, Leffler H, et al. Crystallization and preliminary X-ray diffraction analysis of the human dimeric S-Lac lectin (L-14-II). J Mol Biol. 1993;233(3):553-5.
Lobsanov, Y. D., Gitt, M. A., Leffler, H., Barondes, S., & Rini, J. M. (1993). Crystallization and preliminary X-ray diffraction analysis of the human dimeric S-Lac lectin (L-14-II). Journal of Molecular Biology, 233(3), 553-5.
Lobsanov YD, et al. Crystallization and Preliminary X-ray Diffraction Analysis of the Human Dimeric S-Lac Lectin (L-14-II). J Mol Biol. 1993 Oct 5;233(3):553-5. PubMed PMID: 8411163.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray diffraction analysis of the human dimeric S-Lac lectin (L-14-II). AU - Lobsanov,Y D, AU - Gitt,M A, AU - Leffler,H, AU - Barondes,S, AU - Rini,J M, PY - 1993/10/5/pubmed PY - 1993/10/5/medline PY - 1993/10/5/entrez SP - 553 EP - 5 JF - Journal of molecular biology JO - J Mol Biol VL - 233 IS - 3 N2 - The human recombinant S-Lac lectin, L-14-II, produced in an Escherichia coli expression system, has been co-crystallized in the presence of lactose by the hanging drop vapor diffusion method. The crystals grow in space group P2(1)2(1)2(1) with unit cell dimensions of a = 43.6 A, b = 57.8 A, c = 108.2 A, with a dimer in the asymmetric unit. On a conventional rotating anode the crystals diffract to at least 2.8 A resolution. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/8411163/Crystallization_and_preliminary_X_ray_diffraction_analysis_of_the_human_dimeric_S_Lac_lectin__L_14_II__ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(83)71533-0 DB - PRIME DP - Unbound Medicine ER -