Purification, crystallization and preliminary X-ray diffraction analysis of the putative ABC transporter ATP-binding protein from Thermotoga maritima.
Adenosine triphosphate (ATP) binding cassette transporters (ABC transporters) are ATP hydrolysis-dependent transmembrane transporters. Here, the overproduction, purification and crystallization of the putative ABC transporter ATP-binding protein TM0222 from Thermotoga maritima are reported. The protein was crystallized in the hexagonal space group P6(4)22, with unit-cell parameters a = b = 148.49, c = 106.96 A, gamma = 120.0 degrees . Assuming the presence of two molecules in the asymmetric unit, the calculated V(M) is 2.84 A(3) Da(-1), which corresponds to a solvent content of 56.6%. A three-wavelength MAD data set was collected to 2.3 A resolution from SeMet-substituted TM0222 crystals. Data sets were collected on the BL38B1 beamline at SPring-8, Japan.
Ethayathulla
Abdul S
AS
Department of Biophysics, All India Institute of Medical Sciences, Ansari Nagar, New Delhi 110 029, India.
Bessho
Yoshitaka
Y
Shinkai
Akeo
A
Padmanabhan
Balasundaram
B
Singh
Tej P
TP
Kaur
Punit
P
Yokoyama
Shigeyuki
S
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics; D005822:Genetic Vectors; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D021141:Nucleic Acid Amplification Techniques; D017434:Protein Structure, Tertiary; D020124:Thermotoga maritima / Q000737:chemistry*; D014961:X-Ray Diffraction
D018528:ATP-Binding Cassette Transporters