Crystallization and preliminary structure analysis of CobE, an essential protein of cobalamin (vitamin B12) biosynthesis

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Jitka VévodováKeith S Wilson

Abstract

CobE, a protein implicated in vitamin B12 biosynthesis, from Pseudomonas aeruginosa has been overexpressed in Escherichia coli, purified and crystallized using hanging-drop vapour diffusion. The crystals belong to the primitive orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 31.86, b = 41.07, c = 87.41 A. The diffraction extends to a resolution of 1.9 A. There is one molecule per asymmetric unit and the estimated solvent content is 35%. SeMet-labelled CobE has been prepared and crystallizes under the same conditions as the native protein with diffraction to 1.7 A. The anomalous measurements will be used for phasing.

References

Dec 1, 1990·Trends in Biochemical Sciences·M J Warren, A I Scott
Apr 28, 1968·Journal of Molecular Biology·B W Matthews
Aug 28, 2002·Natural Product Reports·Martin J WarrenJorge C Escalante-Semerena

❮ Previous
Next ❯

Citations

Oct 9, 2012·Nature Chemical Biology·Evelyne DeeryMartin J Warren
May 24, 2012·Biochemical Society Transactions·Simon J Moore, Martin J Warren

❮ Previous
Next ❯

Related Concepts

Related Feeds

Bacterial Protein Structures

Bacterial protein structures can expedite the development of novel antibiotics. Here is the latest research on bacterial proteins and the resolution of their structures.

Bacterial Protein Structures (ASM)

Bacterial protein structures can expedite the development of novel antibiotics. Here is the latest research on bacterial proteins and the resolution of their structures.