Crystallization and preliminary X-ray investigation of recombinant simian immunodeficiency virus proteinase.
Simian immunodeficiency virus (SIV) proteinase has been crystallized from sodium acetate buffer with sodium chloride as precipitant. The crystals are orthorhombic and the space group is C222(1) with unit cell dimensions a = 32.18 A, b = 62.52 A, c = 95.76 A, alpha = beta = gamma = 90 degrees, indicating a single monomer of 10 kDa in the asymmetric unit. The crystals grow to dimensions of 0.2 mm x 0.2 mm x 0.07 mm within a week and are stable in the X-ray beam for at least 50 hours. A different crystal lattice was observed for SIV proteinase crystallized in the presence of pepstatin. The space group was P2(1)2(1)2(1) with cell dimensions of a = 35.26 A, b = 58.59 A, c = 93.95 A, alpha = beta = gamma = 90 degrees. Diffraction beyond 1.7 A was observed, indicating that a high resolution structure analysis is feasible.
Wilderspin
A F
AF
Department of Crystallography, Birbeck College, London, U.K.
Sugrue
R J
RJ
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D003460:Crystallization; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D015302:Simian Immunodeficiency Virus / Q000201:enzymology*; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D016282:Aspartic Acid Endopeptidases; C077164:SIV(mac) proteinase