Structural highlights
Publication Abstract from PubMed
Aqualysin I, a thermostable protease found in the culture medium of Thermus aquaticus YT-1, has been purified to homogeneity using a combination of ion-exchange and affinity chromatography. It is a polypeptide with a molecular weight of 28 350 [Kwon, Terada, Matsuzawa & Ohta (1988). Eur. J. Biochem. 173, 491-497] and is most active at 343-353 K and pH about 10.0 [Matsuzawa, Tokugawa, Hamaoki, Mizoguchi, Taguchi, Terada, Kwon & Ohta (1988). Eur. J. Biochem. 171, 441-447]. Crystals of the enzyme are monoclinic, space group P2(1), with cell dimensions a = 40.80 (5), b = 64.39 (6), c = 45.51 (6) A and beta = 109.1 (1) degrees. The asymmetric unit consists of a single molecule (V(m) = 1.99 A(3)Da(-1)). The crystals are stable to X-radiation and scatter to at least 2.8 A resolution.
Purification, crystallization and preliminary X-ray investigation of aqualysin I, a heat-stable serine protease.,Green PR, Oliver JD, Strickland LC, Toerner DR, Matsuzawa H, Ohta T Acta Crystallogr D Biol Crystallogr. 1993 May 1;49(Pt 3):349-52. PMID:15299524[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Green PR, Oliver JD, Strickland LC, Toerner DR, Matsuzawa H, Ohta T. Purification, crystallization and preliminary X-ray investigation of aqualysin I, a heat-stable serine protease. Acta Crystallogr D Biol Crystallogr. 1993 May 1;49(Pt 3):349-52. PMID:15299524 doi:10.1107/S0907444992012083
