Crystallization of human neutrophil elastase

Human neutrophil elastase was inactivated by methoxysuccinyl-L-Ala-L-Ala-L-Pro-L-Ala-chloromethane. The modified enzyme was crystallized from 40 mM ammonium phosphate, pH 7.0 in the hexagonal space group P6(3) with unit cell parameters a = 74.53 A, b = 74.53 A, c = 70.88 A, alpha = beta = 90 degrees...

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Bibliographic Details
Published in:The Journal of biological chemistry 1987-12, Vol.262 (35), p.17178-17181
Main Authors: Williams, H R, Lin, T Y, Navia, M A, Springer, J P, McKeever, B M, Hoogsteen, K, Dorn, C P
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Crystallization
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Humans
Hydrolases
leukocyte elastase
Neutrophils - enzymology
Pancreatic Elastase
X-Ray Diffraction
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Summary:Human neutrophil elastase was inactivated by methoxysuccinyl-L-Ala-L-Ala-L-Pro-L-Ala-chloromethane. The modified enzyme was crystallized from 40 mM ammonium phosphate, pH 7.0 in the hexagonal space group P6(3) with unit cell parameters a = 74.53 A, b = 74.53 A, c = 70.88 A, alpha = beta = 90 degrees, gamma = 120 degrees. These crystals were resistant to radiation damage and diffracted beyond 1.84-A resolution. The asymmetric unit contained one 25,000-dalton monomer of human neutrophil elastase. Crystals were also grown from the enzyme modified with the analogous iodinated inactivator, p-iodoanilinosuccinyl-L-Ala-L-Ala-L-Pro-L-Ala-chloromethane. These crystals proved to be isomorphous with those of methoxysuccinyl-L-Ala-L-Ala-L-Pro-L-Ala-chloromethane-modified human neutrophil elastase, and served as a single-site, heavy atom derivative for solving the tertiary structure of the enzyme.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)45507-X