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Purification, crystallization, and preliminary X-ray analysis of PepX, an X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis.
Proteins. 1995 Oct; 23(2):278-81.P

Abstract

The X-prolyl dipeptidyl aminopeptidase PepX, a serine peptidase isolated originally from Lactococcus lactis subsp lactis NCDO 763, was cloned and overproduced in Escherichia coli. The enzyme was isolated in its active form in two purification steps. Crystals of PepX were grown by the hanging drop vapor diffusion method using polyethyleneglycol 4000 as precipitant at pH 5.0. The crystals are orthorhombic with cell dimensions a = 92.8 A, b = 102.6 A, and c = 101.6 A, space group P2(1)2(1)2, and probably contain one monomer of 87.5 kDa in the asymmetric unit. The crystals, very stable under X-rays, diffract to at least 2.2 A and are suitable for high-resolution structural analysis.

Authors+Show Affiliations

Chich JF
Unité de Biochimie et de Structure des Protéines, INRA, Centre de Recherches de Jouy-en-Josas, France.
Rigolet P
No affiliation info available
Nardi M
No affiliation info available
Gripon JC
No affiliation info available
Ribadeau-Dumas B
No affiliation info available
Brunie S
No affiliation info available

MeSH

Amino Acid SequenceBacterial ProteinsCloning, MolecularCrystallizationCrystallography, X-RayDipeptidyl-Peptidases and Tripeptidyl-PeptidasesEscherichia coliLactococcus lactisMolecular Sequence DataRecombinant Fusion Proteins

Pub Type(s)

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

Language

eng

PubMed ID

8592708

Citation

Chich, J F., et al. "Purification, Crystallization, and Preliminary X-ray Analysis of PepX, an X-prolyl Dipeptidyl Aminopeptidase From Lactococcus Lactis." Proteins, vol. 23, no. 2, 1995, pp. 278-81.
Chich JF, Rigolet P, Nardi M, et al. Purification, crystallization, and preliminary X-ray analysis of PepX, an X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis. Proteins. 1995;23(2):278-81.
Chich, J. F., Rigolet, P., Nardi, M., Gripon, J. C., Ribadeau-Dumas, B., & Brunie, S. (1995). Purification, crystallization, and preliminary X-ray analysis of PepX, an X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis. Proteins, 23(2), 278-81.
Chich JF, et al. Purification, Crystallization, and Preliminary X-ray Analysis of PepX, an X-prolyl Dipeptidyl Aminopeptidase From Lactococcus Lactis. Proteins. 1995;23(2):278-81. PubMed PMID: 8592708.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, crystallization, and preliminary X-ray analysis of PepX, an X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis. AU - Chich,J F, AU - Rigolet,P, AU - Nardi,M, AU - Gripon,J C, AU - Ribadeau-Dumas,B, AU - Brunie,S, PY - 1995/10/1/pubmed PY - 1995/10/1/medline PY - 1995/10/1/entrez SP - 278 EP - 81 JF - Proteins JO - Proteins VL - 23 IS - 2 N2 - The X-prolyl dipeptidyl aminopeptidase PepX, a serine peptidase isolated originally from Lactococcus lactis subsp lactis NCDO 763, was cloned and overproduced in Escherichia coli. The enzyme was isolated in its active form in two purification steps. Crystals of PepX were grown by the hanging drop vapor diffusion method using polyethyleneglycol 4000 as precipitant at pH 5.0. The crystals are orthorhombic with cell dimensions a = 92.8 A, b = 102.6 A, and c = 101.6 A, space group P2(1)2(1)2, and probably contain one monomer of 87.5 kDa in the asymmetric unit. The crystals, very stable under X-rays, diffract to at least 2.2 A and are suitable for high-resolution structural analysis. SN - 0887-3585 UR - https://www.unboundmedicine.com/medline/citation/8592708/Purification_crystallization_and_preliminary_X_ray_analysis_of_PepX_an_X_prolyl_dipeptidyl_aminopeptidase_from_Lactococcus_lactis_ L2 - https://doi.org/10.1002/prot.340230216 DB - PRIME DP - Unbound Medicine ER -