Tags

Type your tag names separated by a space and hit enter

Purification, crystallization and preliminary X-ray diffraction analysis of human enolase-phosphatase E1.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 01; 61(Pt 5):521-3.AC

Abstract

Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous methionine-salvage pathway and catalyzes the continuous reaction of 2,3-diketo-5-methylthio-1-phosphopentane to yield the acireductone metabolite. Recombinant human E1 enzyme has been crystallized using the hanging-drop vapour-diffusion method and diffraction-quality crystals were grown at 291 K using PEG 4000 as precipitant. Diffraction data were collected to 1.7 A resolution from SeMet-derivative crystals at 100 K using synchrotron radiation. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 54.02, b = 57.55, c = 87.32 A. The structure was subsequently solved by the multi-wavelength anomalous diffraction (MAD) phasing method.

Authors+Show Affiliations

Laboratory of Structural Biology, Tsinghua University, Beijing 100084, People's Republic of China.No affiliation info availableNo affiliation info availableNo 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

16511085

Citation

Wang, Hui, et al. "Purification, Crystallization and Preliminary X-ray Diffraction Analysis of Human Enolase-phosphatase E1." Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 61, no. Pt 5, 2005, pp. 521-3.
Wang H, Pang H, Ding Y, et al. Purification, crystallization and preliminary X-ray diffraction analysis of human enolase-phosphatase E1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005;61(Pt 5):521-3.
Wang, H., Pang, H., Ding, Y., Li, Y., Wu, X., & Rao, Z. (2005). Purification, crystallization and preliminary X-ray diffraction analysis of human enolase-phosphatase E1. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 61(Pt 5), 521-3.
Wang H, et al. Purification, Crystallization and Preliminary X-ray Diffraction Analysis of Human Enolase-phosphatase E1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt 5):521-3. PubMed PMID: 16511085.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, crystallization and preliminary X-ray diffraction analysis of human enolase-phosphatase E1. AU - Wang,Hui, AU - Pang,Hai, AU - Ding,Yi, AU - Li,Yi, AU - Wu,Xiao'ai, AU - Rao,Zihe, Y1 - 2005/04/28/ PY - 2004/10/15/received PY - 2005/04/18/accepted PY - 2006/3/3/pubmed PY - 2006/6/20/medline PY - 2006/3/3/entrez SP - 521 EP - 3 JF - Acta crystallographica. Section F, Structural biology and crystallization communications JO - Acta Crystallogr Sect F Struct Biol Cryst Commun VL - 61 IS - Pt 5 N2 - Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous methionine-salvage pathway and catalyzes the continuous reaction of 2,3-diketo-5-methylthio-1-phosphopentane to yield the acireductone metabolite. Recombinant human E1 enzyme has been crystallized using the hanging-drop vapour-diffusion method and diffraction-quality crystals were grown at 291 K using PEG 4000 as precipitant. Diffraction data were collected to 1.7 A resolution from SeMet-derivative crystals at 100 K using synchrotron radiation. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 54.02, b = 57.55, c = 87.32 A. The structure was subsequently solved by the multi-wavelength anomalous diffraction (MAD) phasing method. SN - 1744-3091 UR - https://www.unboundmedicine.com/medline/citation/16511085/Purification_crystallization_and_preliminary_X_ray_diffraction_analysis_of_human_enolase_phosphatase_E1_ L2 - http://scripts.iucr.org/cgi-bin/paper?S174430910501184X DB - PRIME DP - Unbound Medicine ER -