Human procathepsin L has been expressed in the yeast Pichiapastoris and its inactive (Cys25Ser) and unglycosylated (ThrllOAla) mutant purified, concentrated to 4 mglml, and crystallized by vapor diffusion against solution containing 1.4 M (Na,K)PO, buffer, pH 7.8. Crystal size was increased by multi
Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: Tetrahydromethanopterin formyltransferase fromMethanopyrus kandleri
β Scribed by Shima, Seigo; Thauer, Rudolf K.; Michel, Hartmut; Ermler, Ulrich
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 315 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0887-3585
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β¦ Synopsis
Formy1methanofuran:tetrahydromethanopterin formyltransferase from the hyperthermophilic methanogenic Archaeon Methampyrus kandleri (growth temperature optimum 98Β°C) was crystallized by vapor diffusion methods. Crystal form M obtained with 2-methyl-2,4-pentanediol as precipitant displayed the space group P2, with unit cell parameters o f a = 87.0A, b = 75.4hi,c = 104.7A, and f3 = 113.9" a n d diffracted better than 2 hi resolution. Crystal form P grown from polyethylene glycol 8000 belonged to the space group 14'22 and had unit cell parameters of 157.5 A and 242.1 hi. Diffraction data to 1.73 A were recorded. Crystal form S which was crystallized from (NH,),SO, in the space group 14'22 with unit cell parameters of 151.3 A and 249.5 A diffracted at least to 2.2 hi resolution. All crystal forms probably have four molecules per asymmetric unit and are suitable for X-ray structure analysis. o 1996 Wiley-Liss, hc.
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