Crystallization, data collection and data processing of maltose-binding protein (MalE) from the phytopathogen Xanthomonas axonopodis pv. citri.
نویسندگان
چکیده
Maltose-binding protein is the periplasmic component of the ABC transporter responsible for the uptake of maltose/maltodextrins. The Xanthomonas axonopodis pv. citri maltose-binding protein MalE has been crystallized at 293 K using the hanging-drop vapour-diffusion method. The crystal belonged to the primitive hexagonal space group P6(1)22, with unit-cell parameters a = 123.59, b = 123.59, c = 304.20 A, and contained two molecules in the asymetric unit. It diffracted to 2.24 A resolution.
منابع مشابه
شباهت الگوی الکتروفورز پروتئین استرینهای Xanthomonas axonopodis pv. citri جداشده از مرکبات استانهای هرمزگان وکرمان با استرینهای برخی دیگر از گونههای Xanthomonas
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Protein electrophoretic pattern similarity among 21 strains of Xanthomonas axonopodis pv. citri isolated from Hormozgan and Kerman provinces together with the representatives of reference strains of X.a. pv. citri and X. a. pv. aurantifoli and 246 strains of the other Xanthomonas spp. including : X. a. pv. citri, X. a. pv. glycins, X. a. pv. manihotis, X. c. pv. campestris, X. a. pv. phaseoli, ...
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ورودعنوان ژورنال:
- Acta crystallographica. Section F, Structural biology and crystallization communications
دوره 65 Pt 2 شماره
صفحات -
تاریخ انتشار 2009