|
type |
Journal Article |
authors |
van Straaten KE, Langill DM, Palmer DR, Sanders DA |
title |
Purification, crystallization and preliminary X-ray analysis of NtdA, a putative pyridoxal phosphate-dependent aminotransferase from Bacillus subtilis. |
journal |
Acta Crystallogr Sect F Struct Biol Cryst Commun. |
Activity |
2.6.1.104 |
Family |
2.6.1.104 |
sel |
unselected |
ui |
19342798 |
year |
(2009) |
volume |
65 |
number |
4 |
pages |
426-9 |
| |
abstract |
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 A resolution at the Canadian Light Source (CLS). The crystals belonged to space group P2(1), with unit-cell parameters a = 50.3, b = 106.7, c = 96.7 A, beta = 96.2 degrees, and contained two molecules per asymmetric unit. |
last changed |
2014/08/19 12:51 |
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