Crystallization and preliminary X-ray crystallographic studies of the plant aspartic proteinase cardosin A.
The plant aspartic proteinase cardosin A was crystallized using vapour diffusion. Crystals belong to the monoclinic space group C2, cell dimensions a = 116.9 (2), b = 87.2 (8), c = 81.3 (1) A, beta = 104.4 (4) degrees, and contain two molecules in the asymmetric unit related by a non-crystallographic twofold axis. Diffraction data were collected at room temperature with radiation from a synchrotron source up to 2.85 A resolution. When the crystals were flash cooled to 110 K in a nitrogen stream the same resolution limit could also be obtained on a rotating-anode source. Recently, synchrotron radiation together with flash cooling led to an improvement of the diffraction data to 1.72 A resolution.
Bento
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Instituto de Tecnologia Química e Biológica, Apartado 127, 2780-Oeiras, Portugal.
Frazão
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Coelho
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Wilson
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Dauter
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Carrondo
M A
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D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation
D010940:Plant Proteins; D016282:Aspartic Acid Endopeptidases; C097455:aspartic proteinases, Cynara cardunculus