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Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase alpha-subunits from Escherichia coli.
Mol Cells. 2005 Apr 30; 19(2):219-22.MC

Abstract

The alpha-subunit of Escherichia coli tryptophan synthase (aTS), a component of the tryptophan synthase alpha2beta2 complex, is a monomeric 268-residues protein (Mr = 28,600). alphaTS by itself catalyzes the cleavage of indole-3-glycerol phosphate to glyceraldehyde-3-phosphate and indole, which is converted to tryptophan in tryptophan biosynthesis. Wild-type and P28L/Y173F double mutant alpha-subunits were overexpressed in E. coli and crystallized at 298 K by the hanging-drop vapor-diffusion method. X-ray diffraction data were collected to 2.5 angstroms resolution from the wild-type crystals and to 1.8 angstroms from the crystals of the double mutant, since the latter produced better quality diffraction data. The wild-type crystals belonged to the monoclinic space group C2 (a = 155.64 angstroms, b = 44.54 angstroms, c = 71.53 angstroms and beta = 96.39 degrees) and the P28L/Y173F crystals to the monoclinic space group P21 (a = 71.09 angstroms, b = 52.70, c = 71.52 angstroms, and beta = 91.49 degrees). The asymmetric unit of both structures contained two molecules of aTS. Crystal volume per protein mass (V(m)) and solvent content were 2.15 angstroms3 Da(-1) and 42.95% for the wild-type and 2.34 angstroms3 Da(-1) and 47.52% for the double mutant.

Authors+Show Affiliations

Jeong MS
Korea Nanobiotechnology Center, Pusan National University, Busan 609-735, Korea.
Jang SB
No affiliation info available

MeSH

Amino Acid SequenceCrystallizationCrystallography, X-RayEscherichia coliMolecular Sequence DataMutationProtein SubunitsSequence Homology, Amino AcidTryptophan Synthase

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15879705

Citation

Jeong, Mi Suk, and Se Bok Jang. "Crystallization and X-ray Crystallographic Studies of Wild-type and Mutant Tryptophan Synthase Alpha-subunits From Escherichia Coli." Molecules and Cells, vol. 19, no. 2, 2005, pp. 219-22.
Jeong MS, Jang SB. Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase alpha-subunits from Escherichia coli. Mol Cells. 2005;19(2):219-22.
Jeong, M. S., & Jang, S. B. (2005). Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase alpha-subunits from Escherichia coli. Molecules and Cells, 19(2), 219-22.
Jeong MS, Jang SB. Crystallization and X-ray Crystallographic Studies of Wild-type and Mutant Tryptophan Synthase Alpha-subunits From Escherichia Coli. Mol Cells. 2005 Apr 30;19(2):219-22. PubMed PMID: 15879705.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase alpha-subunits from Escherichia coli. AU - Jeong,Mi Suk, AU - Jang,Se Bok, PY - 2005/5/10/pubmed PY - 2005/10/7/medline PY - 2005/5/10/entrez SP - 219 EP - 22 JF - Molecules and cells JO - Mol Cells VL - 19 IS - 2 N2 - The alpha-subunit of Escherichia coli tryptophan synthase (aTS), a component of the tryptophan synthase alpha2beta2 complex, is a monomeric 268-residues protein (Mr = 28,600). alphaTS by itself catalyzes the cleavage of indole-3-glycerol phosphate to glyceraldehyde-3-phosphate and indole, which is converted to tryptophan in tryptophan biosynthesis. Wild-type and P28L/Y173F double mutant alpha-subunits were overexpressed in E. coli and crystallized at 298 K by the hanging-drop vapor-diffusion method. X-ray diffraction data were collected to 2.5 angstroms resolution from the wild-type crystals and to 1.8 angstroms from the crystals of the double mutant, since the latter produced better quality diffraction data. The wild-type crystals belonged to the monoclinic space group C2 (a = 155.64 angstroms, b = 44.54 angstroms, c = 71.53 angstroms and beta = 96.39 degrees) and the P28L/Y173F crystals to the monoclinic space group P21 (a = 71.09 angstroms, b = 52.70, c = 71.52 angstroms, and beta = 91.49 degrees). The asymmetric unit of both structures contained two molecules of aTS. Crystal volume per protein mass (V(m)) and solvent content were 2.15 angstroms3 Da(-1) and 42.95% for the wild-type and 2.34 angstroms3 Da(-1) and 47.52% for the double mutant. SN - 1016-8478 UR - https://www.unboundmedicine.com/medline/citation/15879705/Crystallization_and_X_ray_crystallographic_studies_of_wild_type_and_mutant_tryptophan_synthase_alpha_subunits_from_Escherichia_coli_ DB - PRIME DP - Unbound Medicine ER -