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Purification, crystallization and preliminary crystallographic analysis of the glycine-cleavage system component T-protein from Pyrococcus horikoshii OT3.
Acta Crystallogr D Biol Crystallogr. 2004 Aug; 60(Pt 8):1450-2.AC

Abstract

The glycine-cleavage system component T-protein is a folate-dependent enzyme that catalyzes the formation of ammonia and 5,10-CH2-tetrahydrofolate from the aminomethyl intermediate bound to the lipoate cofactor of H-protein. T-protein from Pyrococcus horikoshii OT3 has been cloned, overexpressed in Escherichia coli, purified and crystallized by the microbatch method using PEG 4000 as a precipitant at 296 K. X-ray diffraction data have been collected to 1.50 A resolution at 100 K using synchrotron radiation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 78.980, b = 95.708, c = 118.331 A. Assuming one homodimer per asymmetric unit gives a VM value of 2.4 A3 Da(-1) and a solvent content of 49.0%.

Authors+Show Affiliations

Highthroughput Factory, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

15272174

Citation

Lokanath, Neratur K., et al. "Purification, Crystallization and Preliminary Crystallographic Analysis of the Glycine-cleavage System Component T-protein From Pyrococcus Horikoshii OT3." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 8, 2004, pp. 1450-2.
Lokanath NK, Kuroishi C, Okazaki N, et al. Purification, crystallization and preliminary crystallographic analysis of the glycine-cleavage system component T-protein from Pyrococcus horikoshii OT3. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 8):1450-2.
Lokanath, N. K., Kuroishi, C., Okazaki, N., & Kunishima, N. (2004). Purification, crystallization and preliminary crystallographic analysis of the glycine-cleavage system component T-protein from Pyrococcus horikoshii OT3. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 8), 1450-2.
Lokanath NK, et al. Purification, Crystallization and Preliminary Crystallographic Analysis of the Glycine-cleavage System Component T-protein From Pyrococcus Horikoshii OT3. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 8):1450-2. PubMed PMID: 15272174.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, crystallization and preliminary crystallographic analysis of the glycine-cleavage system component T-protein from Pyrococcus horikoshii OT3. AU - Lokanath,Neratur K, AU - Kuroishi,Chizu, AU - Okazaki,Nobuo, AU - Kunishima,Naoki, Y1 - 2004/07/21/ PY - 2004/04/05/received PY - 2004/05/27/accepted PY - 2004/7/24/pubmed PY - 2005/2/19/medline PY - 2004/7/24/entrez SP - 1450 EP - 2 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 8 N2 - The glycine-cleavage system component T-protein is a folate-dependent enzyme that catalyzes the formation of ammonia and 5,10-CH2-tetrahydrofolate from the aminomethyl intermediate bound to the lipoate cofactor of H-protein. T-protein from Pyrococcus horikoshii OT3 has been cloned, overexpressed in Escherichia coli, purified and crystallized by the microbatch method using PEG 4000 as a precipitant at 296 K. X-ray diffraction data have been collected to 1.50 A resolution at 100 K using synchrotron radiation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 78.980, b = 95.708, c = 118.331 A. Assuming one homodimer per asymmetric unit gives a VM value of 2.4 A3 Da(-1) and a solvent content of 49.0%. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15272174/Purification_crystallization_and_preliminary_crystallographic_analysis_of_the_glycine_cleavage_system_component_T_protein_from_Pyrococcus_horikoshii_OT3_ DB - PRIME DP - Unbound Medicine ER -