Tags

Type your tag names separated by a space and hit enter

Purification, crystallization, and preliminary x-ray studies of a bifunctional 5,10-methenyl/methylene-tetrahydrofolate cyclohydrolase/dehydrogenase from Escherichia coli.
Proteins. 1997 Feb; 27(2):322-4.P

Abstract

A bifunctional enzyme that catalyzes the conversion of formyltetrahydrofolate to methylene-tetrahydrofolate (5,10-methenyltetrahydrofolate cyclohydrolase and 5,10-methylene tetrahydrofolate dehydrogenase), has been subcloned from a cDNA library, purified to homogeneity, and crystallized. The crystals belong to space group I222, with unit cell dimensions of a = 64.5 A, b = 84.9 A, c = 146.1 A. The crystal unit cell and diffraction is consistent with an asymmetric unit consisting of the enzyme monomer, and a specific volume of the unit cell of 3.2 A3/Da. The crystals diffract to at least 2.8 A resolution after flash-cooling, when using a rotating anode x-ray source and an RAXIS image plate detector. A 2.56 A resolution native data set has been collected at beamline X12-C at the NSLS.

Authors+Show Affiliations

Cheung E
Department of Molecular and Cell Biology, University of California, Berkeley, USA.
D'Ari L
No affiliation info available
Rabinowitz JC
No affiliation info available
Dyer DH
No affiliation info available
Huang JY
No affiliation info available
Stoddard BL
No affiliation info available

MeSH

AminohydrolasesBacterial ProteinsCloning, MolecularCrystallography, X-RayEscherichia coliMethylenetetrahydrofolate Dehydrogenase (NADP)Multienzyme Complexes

Pub Type(s)

Journal Article

Language

eng

PubMed ID

9061797

Citation

Cheung, E, et al. "Purification, Crystallization, and Preliminary X-ray Studies of a Bifunctional 5,10-methenyl/methylene-tetrahydrofolate Cyclohydrolase/dehydrogenase From Escherichia Coli." Proteins, vol. 27, no. 2, 1997, pp. 322-4.
Cheung E, D'Ari L, Rabinowitz JC, et al. Purification, crystallization, and preliminary x-ray studies of a bifunctional 5,10-methenyl/methylene-tetrahydrofolate cyclohydrolase/dehydrogenase from Escherichia coli. Proteins. 1997;27(2):322-4.
Cheung, E., D'Ari, L., Rabinowitz, J. C., Dyer, D. H., Huang, J. Y., & Stoddard, B. L. (1997). Purification, crystallization, and preliminary x-ray studies of a bifunctional 5,10-methenyl/methylene-tetrahydrofolate cyclohydrolase/dehydrogenase from Escherichia coli. Proteins, 27(2), 322-4.
Cheung E, et al. Purification, Crystallization, and Preliminary X-ray Studies of a Bifunctional 5,10-methenyl/methylene-tetrahydrofolate Cyclohydrolase/dehydrogenase From Escherichia Coli. Proteins. 1997;27(2):322-4. PubMed PMID: 9061797.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, crystallization, and preliminary x-ray studies of a bifunctional 5,10-methenyl/methylene-tetrahydrofolate cyclohydrolase/dehydrogenase from Escherichia coli. AU - Cheung,E, AU - D'Ari,L, AU - Rabinowitz,J C, AU - Dyer,D H, AU - Huang,J Y, AU - Stoddard,B L, PY - 1997/2/1/pubmed PY - 2000/6/20/medline PY - 1997/2/1/entrez SP - 322 EP - 4 JF - Proteins JO - Proteins VL - 27 IS - 2 N2 - A bifunctional enzyme that catalyzes the conversion of formyltetrahydrofolate to methylene-tetrahydrofolate (5,10-methenyltetrahydrofolate cyclohydrolase and 5,10-methylene tetrahydrofolate dehydrogenase), has been subcloned from a cDNA library, purified to homogeneity, and crystallized. The crystals belong to space group I222, with unit cell dimensions of a = 64.5 A, b = 84.9 A, c = 146.1 A. The crystal unit cell and diffraction is consistent with an asymmetric unit consisting of the enzyme monomer, and a specific volume of the unit cell of 3.2 A3/Da. The crystals diffract to at least 2.8 A resolution after flash-cooling, when using a rotating anode x-ray source and an RAXIS image plate detector. A 2.56 A resolution native data set has been collected at beamline X12-C at the NSLS. SN - 0887-3585 UR - https://www.unboundmedicine.com/medline/citation/9061797/Purification_crystallization_and_preliminary_x_ray_studies_of_a_bifunctional_510_methenyl/methylene_tetrahydrofolate_cyclohydrolase/dehydrogenase_from_Escherichia_coli_ L2 - https://doi.org/10.1002/(sici)1097-0134(199702)27:2<322::aid-prot19>3.0.co;2-o DB - PRIME DP - Unbound Medicine ER -
Grapherence [↓1]

Related Citations

More