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Crystallization and preliminary X-ray diffraction studies of the human adenovirus serotype 2 proteinase with peptide cofactor

✍ Scribed by Lisa J. Keefe; Stephan L. Ginell; Edwin M. Westbrook; Carl W. Anderson

Publisher
Cold Spring Harbor Laboratory Press
Year
1995
Tongue
English
Weight
361 KB
Volume
4
Category
Article
ISSN
0961-8368

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✦ Synopsis

Abstract

Recombinant human adenovirus serotype 2 proteinase (both native and selenomethionine‐substituted) has been crystallized in the presence of the serotype 12, 11‐residue peptide cofactor. The crystals (space group P3~1~21 or P3~2~21, one molecule per asymmetric unit, a = b = 41.3 Å, c = 197.0 Å) grew in solutions containing 20–40% 2‐methyl‐2,4‐pentanediol (MPD), 0.1–0.2 M sodium citrate, and 0.1 M sodium HEPES, pH 5.0–7.5. Diffraction data (84% complete to 2.2 Å resolution with R~merge~ of 0.0335) have been measured from cryopreserved native enzyme crystals with the Argonne blue (1,024 × 1,024 pixel array) charge‐coupled device detector at beamline X8C at the National Synchrotron Light Source (operated by Argonne National Laboratory's Structural Biology Center). Additionally, diffraction data from selenomethionine‐substituted proteinase, 65% complete to 2.0 Å resolution with R~merge~ values ranging 0.05–0.07, have been collected at three X‐ray energies at and near the selenium absorption edge. We have determined three of the six selenium sites and are initiating a structure solution by the method of multiwavelength anomalous diffraction phasing.

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