Crystallization and preliminary X-ray analysis of the E. coli hypothetical protein TdcF.
Crystals of the hypothetical protein TdcF (subunit MW = 14 007) from Escherichia coli were grown by vapour diffusion. The protein crystallizes in space group P2(1)2(1)2, with unit-cell parameters a = 72.67, b = 86.22, c = 62.62 A. Native data to a resolution of 2.35 A were collected from a single crystal at 100 K on a rotating-anode X-ray generator. Preliminary analysis of these data indicated that the asymmetric unit corresponded to a trimer, which was supported by a convincing molecular-replacement solution using the YjgF trimer as the probe structure.
Burman
Julia D
JD
Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, England.
Stevenson
Clare E M
CE
Hauton
Katherine A
KA
Sawers
Gary
G
Lawson
David M
DM
D000595:Amino Acid Sequence; D026921:Amino Acid Transport Systems, Neutral; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012997:Solvents; D014961:X-Ray Diffraction
D026921:Amino Acid Transport Systems, Neutral; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D012997:Solvents; C480728:TdcF protein, E coli