Crystallization and preliminary X-ray crystallographic analysis of carbamoyl phosphate synthetase from Escherichia coli. Academic Article

abstract

• Carbamoyl Phosphate synthetase catalyzes the formation of carbamoyl phosphate, a high-energy intermediate used in several biosynthetic pathways. The enzyme from Escherichia coli has been crystallized at pH 8 in the presence of L-ornithine, MnCl(2) and ADP, using PEG 8000 in combination with NEt(4)Cl and KCl. The crystals (apparently) belong to the orthorhombic space group P2(1)2(1)2(1) with unit-cell dimensions of a = 154.4, b = 166.5 and c = 338.7 A. The crystals are relatively sensitive to radiation damage, but show diffraction to beyond 2.8 A resolution. A low-resolution (3.5 A) native data set has been recorded and conditions for flash cooling the crystal have been established.

authors

• Raushel, Frank

published proceedings

• Acta Crystallogr D Biol Crystallogr

altmetric score

• 3.25

author list (cited authors)

• Thoden, J. B., Raushel, F. M., Mareya, S., Tomchick, D., & Rayment, I.

citation count

• 2

complete list of authors

• Thoden, JB||Raushel, FM||Mareya, S||Tomchick, D||Rayment, I

publication date

• September 1995

publisher

• International Union of Crystallography (IUCr)  Publisher

published in

• Acta Crystallographica Section D: Biological Crystallography  Journal

keywords

• 31 Biological Sciences
• 3101 Biochemistry And Cell Biology

PubMed Central ID

• 15299816

Digital Object Identifier (DOI)

• 10.1107/S0907444994012801

URI

• https://hdl.handle.net/1969.1/185488

start page

• 827

end page

• 829

volume

• 51

issue

• Pt 5

URL

• http://dx.doi.org/10.1107/s0907444994012801