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

✍ Scribed by Alba Guarnéa; Núaria Verdaguer; Ignasi Fita; Regina Kirchweger; Hans-Dieter Liebig; Dieter Blaas; Tim Skern

Publisher
Cold Spring Harbor Laboratory Press
Year
1996
Tongue
English
Weight
260 KB
Volume
5
Category
Article
ISSN
0961-8368

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✦ Synopsis

Abstract

Different 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 MgCl~2~ and PEG 6000 as precipitants. Well‐developed crystals, with cubic morphology growing to approximately 1.0 mm^3^ in size, presented a large unit cell parameter of 274.5 Å and diffracted to, at most, 5 Å 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 × 0.3 × 0.7 mm^3^, diffracted to approximately 4.0 Å resolution, but presented a strong anisotropic mosaicity around the longest crystal axis. Crystals with a needlelike morphology and reaching sizes of about 0.2 × 0.3 × 1.2 mm^3^ diffracted beyond 3.5 Å 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 1222 (or I2~1~2~1~2~1~) and unit cell dimensions a = 65.9 Å, b = 104.3 Å, and c = 124.0 Å, 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%.

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