Crystallization and preliminary X‐ray crystallographic analysis of carbamoyl phosphate synthetase from  Escherichia coli | Zendy

Thoden J. B. | Zendy; Raushel F. M. | Zendy; Mareya S. | Zendy; Tomchick D. R. | Zendy; Rayment I. | Zendy

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Crystallization and preliminary X‐ray crystallographic analysis of carbamoyl phosphate synthetase from Escherichia coli

Author(s) -

Thoden J. B.,

Raushel F. M.,

Mareya S.,

Tomchick D. R.,

Rayment I.

Publication year - 1995

Publication title -

acta crystallographica section d

Language(s) - English

Resource type - Journals

ISSN - 1399-0047

DOI - 10.1107/s0907444994012801

Subject(s) - orthorhombic crystal system , crystallization , escherichia coli , resolution (logic) , phosphate , crystallography , x ray , chemistry , enzyme , stereochemistry , crystal structure , biochemistry , organic chemistry , artificial intelligence , computer science , gene , physics , quantum mechanics

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 P 2 1 2 1 2 1 with unit‐cell dimensions of a = 154.4, b = 166.5 and c = 338.7 Å. The crystals are relatively sensitive to radiation damage, but show diffraction to beyond 2.8 Å resolution. A low‐resolution (3.5 Å) native data set has been recorded and conditions for flash cooling the crystal have been established.

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