ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
Tabtoxin-resistance protein (TTR), an acetyltransferase from Pseudomonas syringae pv. tabaci, was overexpressed in Eschericha coli M15 and the TTR fusion protein complexed with acetyl-coenzyme A (AcCoA) was purified and crystallized. Diffraction data were collected to 3.0 Å resolution in-house and the crystal was found to belong to space group P21, with unit-cell parameters a = 47.6, b = 66.6, c = 53.5 Å, β = 104.3°. Furthermore, a selenomethionine (SeMet) TTR fusion protein derivative was overexpressed in the same expression system and its complex with AcCoA was purified in a reductive environment. The SeMet TTR derivative crystallized in two forms: the first was identical to that observed for native crystals and the second belonged to space group C2, with unit-cell parameters a = 101.7, b = 45.6, c = 84.2 Å, β = 105.8°. Data from the P21 crystal form were collected in-house to 2.3 Å resolution. Subsequently, three different wavelength data sets of the C2 crystal form to 1.55 Å resolution were collected at the Advanced Photon Source at Argonne National Laboratory.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444901014202
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