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Crystallization and preliminary X-ray diffraction studies of the Lb proteinase from foot-and-mouth disease virus

AutorGuarné, Alba; Kirchweger, Regina; Verdaguer, Núria ; Liebig, Hans-Dieter; Blaas, Dieter; Skern, Tim; Fita, Ignacio
Palabras claveCysteine-proteinase
Foot-and-mouth disease virus
Viral proteinase
X-ray crystallography
Fecha de publicaciónsep-1996
EditorCold Spring Harbor Laboratory. Press
CitaciónProtein Science 5(9): 1931-1933 (1996)
ResumenDifferent crystal forms of the C23A mutant from the leader proteinase of foot-and-mouth disease virus were obtained by the hanging drop vapor diffusion technique, using MgCl2 and PEG 6000 as precipitants. Well-developed crystals, with cubic morphology growing to approximately 1.0 mm3 in size, presented a large unit cell parameter of 274.5 A and diffracted to, at most, 5 A resolution. A second type of crystal had a tetragonal appearance and these were obtained in droplets soaked in a silica gel matrix. These crystals, with an approximate size of 0.3 X 0.3 X 0.7 mm3, diffracted to approximately 4.0 A resolution, but presented a strong anisotropic mosaicity around the longest crystal axis. Crystals with a needlelike morphology and reaching sizes of about 0.2 X 0.3 X 1.2 mm3 diffracted beyond 3.5 A resolution and were stable to X-ray radiation for approximately one day when using a conventional source at room temperature. These crystals are orthorhombic with space group I222 (or I2(1)2(1)2(1)) and unit cell dimensions a = 65.9 A, b = 104.3 A, and c = 124.0 A, and appear well suited for high-resolution studies. Density packing considerations are consistent with the presence of two molecules in the asymmetric unit and a solvent content of approximately 54%.
Descripción3 pages, 1 table.-- PMID: 8880919 [PubMed].-- PMCID: PMC2143545.
Versión del editorhttp://dx.doi.org/10.1002/pro.5560050921
ISSN0961-8368 (Print)
1469-896X (Online)
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