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Acta Crystallogr D Biol Crystallogr ; 58(Pt 12): 2138-40, 2002 Dec.
Article in English | MEDLINE | ID: mdl-12454479

ABSTRACT

The ytxM gene product from Bacillus subtilis has been cloned, expressed in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method using PEG 3350 as the precipitant. Multiple-wavelength anomalous dispersive X-ray data have been collected to 2.0 A resolution on a single selenomethionine-incorporated crystal. This crystal belongs to the primitive orthorhombic system, with approximate unit-cell parameters a = 44.3, b = 90.9, c = 136.1 A, alpha = beta = gamma = 90 degrees and two monomers in the asymmetric unit.


Subject(s)
Bacillus subtilis/chemistry , Bacterial Proteins/chemistry , Amino Acid Sequence , Bacillus subtilis/genetics , Bacterial Proteins/genetics , Crystallization , Crystallography, X-Ray , Molecular Sequence Data , Protein Conformation , Sequence Homology, Amino Acid
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