Open AccessPurification, crystallization and preliminary X‐ray analysis of NtdA, a putative pyridoxal phosphate‐dependent aminotransferase from Bacillus subtilis
Author(s) -
Van Straaten K. E.,
Langill D. M.,
Palmer D. R. J.,
Sanders D. A. R.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109009038
Subject(s) - bacillus subtilis , crystallization , pyridoxal phosphate , pyridoxal , enzyme , chemistry , resolution (logic) , affinity chromatography , crystallography , molecule , chromatography , biochemistry , biology , organic chemistry , bacteria , genetics , cofactor , artificial intelligence , computer science
NtdA is a putative sugar aminotransferase that is required for the synthesis of 3,3′‐neotrehalosadiamine. The enzyme was purified to homogeneity by means of Ni 2+ ‐affinity chromatography and was crystallized using the microbatch method. X‐ray diffraction data were collected from a single crystal to 2.3 Å resolution at the Canadian Light Source (CLS). The crystals belonged to space group P 2 1 , with unit‐cell parameters a = 50.3, b = 106.7, c = 96.7 Å, β = 96.2°, and contained two molecules per asymmetric unit.