Crystallization of the aspartylprotease from the human immunodeficiency virus, HIV-1.
The aspartylprotease of the human immunodeficiency virus HIV-1 (NY5) has been crystallized in a form suitable for x-ray diffraction analysis. The crystals are tetragonal bipyramids and produce an x-ray diffraction pattern that exhibits the symmetry associated with space group P4(1)2(1)2 (or its enantiomorph, P4(3)2(1)2). The unit cell parameters are a = b = 50.3 A, c = 106.8 A, alpha = beta = gamma = 90 degrees; measurable diffraction intensities are observed to a resolution of 2.5 A. Density measurements indicate one molecule of 9,400 daltons/asymmetric unit. The symmetry of this space group could accommodate the proposed active dimer species of the protease if the 2-fold axis were coincident with one of the crystallographic 2-fold axes.
McKeever
B M
BM
Department of Biophysical Chemistry, Merck Sharp and Dohme Research Laboratories, Rahway, New Jersey 07065.
Navia
M A
MA
Fitzgerald
P M
PM
Springer
J P
JP
Leu
C T
CT
Heimbach
J C
JC
Herbert
W K
WK
Sigal
I S
IS
Darke
P L
PL
D016282:Aspartic Acid Endopeptidases; D002852:Chromatography, Ion Exchange; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification*; D015497:HIV-1 / Q000201:enzymology*; D008970:Molecular Weight; D014961:X-Ray Diffraction
D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases