Crystallization of the aspartylprotease from the human immunodeficiency virus, HIV-1

• Published in: The Journal of biological chemistry Vol. 264; no. 4; pp. 1919 - 1921
• Main Authors: McKeever, B M, Navia, M A, Fitzgerald, P M D, Springer, J P, Leu, C T, Heimbach, J C, Herbert, W K, Sigal, I S, Darke, P L
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 05.02.1989; American Society for Biochemistry and Molecular Biology
• Subjects: AIDS/HIV; Aspartic Acid Endopeptidases; Biological and medical sciences; Chromatography, Ion Exchange; Crystalline structure; Crystallization; Electrophoresis, Polyacrylamide Gel; Endopeptidases - isolation & purification; Fundamental and applied biological sciences. Psychology; HIV-1 - enzymology; human immunodeficiency virus; Molecular biophysics; Molecular Weight; Structure in molecular biology; X-Ray Diffraction; Virus; Enzyme; Proteinase; Active site; Retroviridae; Human immunodeficiency virus; Crystallography; X ray diffraction; Crystalline structure; Symmetry
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)94119-0

The aspartylprotease of the human immunodeficiency virus HIV-1 (NY5) has been crystallized in a form suitable for x-ray diffraction analysis. The crystals are tetragonal bipyramids and produce an x-ray diffraction pattern that exhibits the symmetry associated with space group P41212 (or its enantiomorph, P43212). The unit cell parameters are a = b = 50.3 Å, c = 106.8 A, α = β = γ = 90 ° measurable diffraction intensities are observed to a resolution of 2.5 A. Density measurements indicate one molecule of 9,400 daltons/asymmetric unit. The symmetry of this space group could accommodate the proposed active dimer species of the protease if the 2-fold axis were coincident with one of the crystallographic 2-fold axes.