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Crystallization, preliminary X-ray diffraction study, and crystal packing of a complex between anti-hen lysozyme antibody F9.13.7 and guinea-fowl lysozyme.
Proteins. 1993 Feb; 15(2):209-12.P

Abstract

The complex formed between the Fab fragment of a murine monoclonal antihen egg lysozyme antibody F9.13.7 and the heterologous antigen Guinea-fowl egg lysozyme has been crystallized by the hanging drop technique. The crystals, which diffract X-rays to 3 A resolution, belong to the monoclinic space group P2(1), with a = 83.7 A, b = 195.5 A, c = 50.2 A, beta = 108.5 degrees and have two molecules of the complex in the asymmetric unit. The three-dimensional structure has been determined from a preliminary data set to 4 A using molecular replacement techniques. The lysozyme-Fab complexes are arranged with their long molecular axes approximately parallel to the crystallographic unique axis. Fab F9.13.7 binds an antigenic determinant that partially overlaps the epitope recognized by antilysozyme antibody HyHEL10.

Authors+Show Affiliations

Unité d'Immunologie Structurale, URA 359 CNRS, Institut Pasteur, Paris, France.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

7680133

Citation

Lescar, J, et al. "Crystallization, Preliminary X-ray Diffraction Study, and Crystal Packing of a Complex Between Anti-hen Lysozyme Antibody F9.13.7 and Guinea-fowl Lysozyme." Proteins, vol. 15, no. 2, 1993, pp. 209-12.
Lescar J, Riottot MM, Souchon H, et al. Crystallization, preliminary X-ray diffraction study, and crystal packing of a complex between anti-hen lysozyme antibody F9.13.7 and guinea-fowl lysozyme. Proteins. 1993;15(2):209-12.
Lescar, J., Riottot, M. M., Souchon, H., Chitarra, V., Bentley, G. A., Navaza, J., Alzari, P. M., & Poljak, R. J. (1993). Crystallization, preliminary X-ray diffraction study, and crystal packing of a complex between anti-hen lysozyme antibody F9.13.7 and guinea-fowl lysozyme. Proteins, 15(2), 209-12.
Lescar J, et al. Crystallization, Preliminary X-ray Diffraction Study, and Crystal Packing of a Complex Between Anti-hen Lysozyme Antibody F9.13.7 and Guinea-fowl Lysozyme. Proteins. 1993;15(2):209-12. PubMed PMID: 7680133.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization, preliminary X-ray diffraction study, and crystal packing of a complex between anti-hen lysozyme antibody F9.13.7 and guinea-fowl lysozyme. AU - Lescar,J, AU - Riottot,M M, AU - Souchon,H, AU - Chitarra,V, AU - Bentley,G A, AU - Navaza,J, AU - Alzari,P M, AU - Poljak,R J, PY - 1993/2/1/pubmed PY - 1993/2/1/medline PY - 1993/2/1/entrez SP - 209 EP - 12 JF - Proteins JO - Proteins VL - 15 IS - 2 N2 - The complex formed between the Fab fragment of a murine monoclonal antihen egg lysozyme antibody F9.13.7 and the heterologous antigen Guinea-fowl egg lysozyme has been crystallized by the hanging drop technique. The crystals, which diffract X-rays to 3 A resolution, belong to the monoclinic space group P2(1), with a = 83.7 A, b = 195.5 A, c = 50.2 A, beta = 108.5 degrees and have two molecules of the complex in the asymmetric unit. The three-dimensional structure has been determined from a preliminary data set to 4 A using molecular replacement techniques. The lysozyme-Fab complexes are arranged with their long molecular axes approximately parallel to the crystallographic unique axis. Fab F9.13.7 binds an antigenic determinant that partially overlaps the epitope recognized by antilysozyme antibody HyHEL10. SN - 0887-3585 UR - https://www.unboundmedicine.com/medline/citation/7680133/Crystallization_preliminary_X_ray_diffraction_study_and_crystal_packing_of_a_complex_between_anti_hen_lysozyme_antibody_F9_13_7_and_guinea_fowl_lysozyme_ L2 - https://doi.org/10.1002/prot.340150211 DB - PRIME DP - Unbound Medicine ER -