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Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase.
Acta Crystallogr D Biol Crystallogr. 2004 Nov; 60(Pt 11):2073-5.AC

Abstract

Tryptophanase from Escherichia coli is a pyridoxal phosphate-dependent homotetrametic enzyme with a subunit weight of 52 kDa. It has been crystallized in the apo form by the hanging-drop vapour-diffusion method using polyethylene glycol 400 as a precipitant and magnesium chloride as an additive. The crystals belong to the orthorhombic space group F222, with unit-cell parameters a = 118.4, b = 120.1, c = 171.2 A. A 97.8% complete data set to 1.9 A resolution was collected at a rotating-anode source from a single frozen crystal. Packing-density considerations agree with a monomer in the asymmetric unit with a solvent content of 55%. Tryptophanase mutants W330F and Y74F were crystallized under the same conditions and the crystals diffracted to a resolution limit of 1.9 A. Data sets of wild-type crystals soaked with L-tryptophan or pyridoxal phosphate were collected, as well as of Y74F mutant soaked with both.

Authors+Show Affiliations

Kogan A
Department of Chemistry, Ben-Gurion University of the Negev, POB 653, Beer-Sheva 84105, Israel.
Gdalevsky GY
No affiliation info available
Cohen-Luria R
No affiliation info available
Parola AH
No affiliation info available
Goldgur Y
No affiliation info available

MeSH

ApoenzymesCrystallizationCrystallography, X-RayEscherichia coliMutationTryptophanTryptophanaseTyrosine

Pub Type(s)

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

Language

eng

PubMed ID

15502331

Citation

Kogan, Anna, et al. "Crystallization and Preliminary X-ray Analysis of the Apo Form of Escherichia Coli Tryptophanase." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 11, 2004, pp. 2073-5.
Kogan A, Gdalevsky GY, Cohen-Luria R, et al. Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 11):2073-5.
Kogan, A., Gdalevsky, G. Y., Cohen-Luria, R., Parola, A. H., & Goldgur, Y. (2004). Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 11), 2073-5.
Kogan A, et al. Crystallization and Preliminary X-ray Analysis of the Apo Form of Escherichia Coli Tryptophanase. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 11):2073-5. PubMed PMID: 15502331.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase. AU - Kogan,Anna, AU - Gdalevsky,Garik Y, AU - Cohen-Luria,Rivka, AU - Parola,Abraham H, AU - Goldgur,Yehuda, Y1 - 2004/10/20/ PY - 2004/07/20/received PY - 2004/09/09/accepted PY - 2004/10/27/pubmed PY - 2005/5/17/medline PY - 2004/10/27/entrez SP - 2073 EP - 5 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 11 N2 - Tryptophanase from Escherichia coli is a pyridoxal phosphate-dependent homotetrametic enzyme with a subunit weight of 52 kDa. It has been crystallized in the apo form by the hanging-drop vapour-diffusion method using polyethylene glycol 400 as a precipitant and magnesium chloride as an additive. The crystals belong to the orthorhombic space group F222, with unit-cell parameters a = 118.4, b = 120.1, c = 171.2 A. A 97.8% complete data set to 1.9 A resolution was collected at a rotating-anode source from a single frozen crystal. Packing-density considerations agree with a monomer in the asymmetric unit with a solvent content of 55%. Tryptophanase mutants W330F and Y74F were crystallized under the same conditions and the crystals diffracted to a resolution limit of 1.9 A. Data sets of wild-type crystals soaked with L-tryptophan or pyridoxal phosphate were collected, as well as of Y74F mutant soaked with both. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15502331/Crystallization_and_preliminary_X_ray_analysis_of_the_apo_form_of_Escherichia_coli_tryptophanase_ DB - PRIME DP - Unbound Medicine ER -