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Crystallization and preliminary X-ray diffraction studies of a monoclonal antibody Fab fragment against foot-and-mouth disease virus and of its complex with the main antigenic site peptide.
Proteins. 1994 Feb; 18(2):201-3.P

Abstract

The Fab fragment of the neutralizing monoclonal antibody SD6 elicited against foot-and-mouth disease virus (FMDV) C-S8c1 and its complex with a peptide, corresponding to the major antigenic site of FMDV (VP1 residues 136-150, YTASARGDLAHLTTT), have been crystallized using the hanging drop vapor diffusion techniques. For the isolated Fab, crystals diffracting to 2.5 A resolution were obtained at room temperature using ammonium sulfate as precipitant. These crystals are monoclinic, space group C2, and unit cell parameters a = 109.53 A, b = 89.12 A, c = 64.04 A, and beta = 112.9 degrees and contain one Fab molecule per asymmetric unit. Crystals from the complex diffract, at least, to 2.8 A resolution and were obtained, at room temperature, using PEG as precipitant. These crystals are monoclinic, space group P2, and unit cell parameters a = 56.11 A, b = 60.67 A, c = 143.45 A, and beta = 95.4 degrees. Density packing considerations indicate that there are two Fab molecules in the asymmetric unit.

Authors+Show Affiliations

Verdaguer N
Departamento de Ingeniería Química, E.T.S.E.I.B., Universidad Politécnica de Cataluña, Barcelona, Spain.
Mateu MG
No affiliation info available
Bravo J
No affiliation info available
Tormo J
No affiliation info available
Giralt E
No affiliation info available
Andreu D
No affiliation info available
Domingo E
No affiliation info available
Fita I
No affiliation info available

MeSH

Amino Acid SequenceAnimalsAntibodies, MonoclonalAntibodies, ViralAntigens, ViralAphthovirusCapsidCapsid ProteinsCrystallography, X-RayImmunoglobulin Fab FragmentsMiceMolecular Sequence DataMolecular StructurePeptide Fragments

Pub Type(s)

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

Language

eng

PubMed ID

8159669

Citation

Verdaguer, N, et al. "Crystallization and Preliminary X-ray Diffraction Studies of a Monoclonal Antibody Fab Fragment Against Foot-and-mouth Disease Virus and of Its Complex With the Main Antigenic Site Peptide." Proteins, vol. 18, no. 2, 1994, pp. 201-3.
Verdaguer N, Mateu MG, Bravo J, et al. Crystallization and preliminary X-ray diffraction studies of a monoclonal antibody Fab fragment against foot-and-mouth disease virus and of its complex with the main antigenic site peptide. Proteins. 1994;18(2):201-3.
Verdaguer, N., Mateu, M. G., Bravo, J., Tormo, J., Giralt, E., Andreu, D., Domingo, E., & Fita, I. (1994). Crystallization and preliminary X-ray diffraction studies of a monoclonal antibody Fab fragment against foot-and-mouth disease virus and of its complex with the main antigenic site peptide. Proteins, 18(2), 201-3.
Verdaguer N, et al. Crystallization and Preliminary X-ray Diffraction Studies of a Monoclonal Antibody Fab Fragment Against Foot-and-mouth Disease Virus and of Its Complex With the Main Antigenic Site Peptide. Proteins. 1994;18(2):201-3. PubMed PMID: 8159669.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray diffraction studies of a monoclonal antibody Fab fragment against foot-and-mouth disease virus and of its complex with the main antigenic site peptide. AU - Verdaguer,N, AU - Mateu,M G, AU - Bravo,J, AU - Tormo,J, AU - Giralt,E, AU - Andreu,D, AU - Domingo,E, AU - Fita,I, PY - 1994/2/1/pubmed PY - 1994/2/1/medline PY - 1994/2/1/entrez SP - 201 EP - 3 JF - Proteins JO - Proteins VL - 18 IS - 2 N2 - The Fab fragment of the neutralizing monoclonal antibody SD6 elicited against foot-and-mouth disease virus (FMDV) C-S8c1 and its complex with a peptide, corresponding to the major antigenic site of FMDV (VP1 residues 136-150, YTASARGDLAHLTTT), have been crystallized using the hanging drop vapor diffusion techniques. For the isolated Fab, crystals diffracting to 2.5 A resolution were obtained at room temperature using ammonium sulfate as precipitant. These crystals are monoclinic, space group C2, and unit cell parameters a = 109.53 A, b = 89.12 A, c = 64.04 A, and beta = 112.9 degrees and contain one Fab molecule per asymmetric unit. Crystals from the complex diffract, at least, to 2.8 A resolution and were obtained, at room temperature, using PEG as precipitant. These crystals are monoclinic, space group P2, and unit cell parameters a = 56.11 A, b = 60.67 A, c = 143.45 A, and beta = 95.4 degrees. Density packing considerations indicate that there are two Fab molecules in the asymmetric unit. SN - 0887-3585 UR - https://www.unboundmedicine.com/medline/citation/8159669/Crystallization_and_preliminary_X_ray_diffraction_studies_of_a_monoclonal_antibody_Fab_fragment_against_foot_and_mouth_disease_virus_and_of_its_complex_with_the_main_antigenic_site_peptide_ DB - PRIME DP - Unbound Medicine ER -
Grapherence [↓2]

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