1vkq

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Revision as of 02:48, 21 November 2007

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spinqualitylabelsall models 1vkq, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

A re-determination of the structure of the triple mutant (K53,56,120M) of phospholipase A2 at 1.6A resolution using sulphur-SAS at 1.54A wavelength

Overview

The crystal structure of the triple mutant K53,56,120M of bovine, pancreatic phospholipase A(2) has been redetermined using sulfur, single-wavelength anomalous scattering. The synchrotron data were, collected at lambda = 1.54 A and the crystal diffracted to 1.6 A, resolution. The program SOLVE was used to locate the heavy atoms and to, estimate the initial phases and the resulting map was then subjected to, RESOLVE. The output of 455 non-H atoms, including 12 S atoms, one calcium, ion and one chloride ion, were then subjected to ARP/wARP followed by, REFMAC. With the improved phases, the automatic model building, successfully built more than 85% of the 123 residues, excluding the N- and, C-terminal residues. The final crystallographic R factor is 17.7% (R(free), = 21.7%). The refined model consists of 954 non-H protein atoms, 165 water, O atoms, three 2-methyl-2,4-pentanediol (MPD) molecules, one calcium ion, and one chloride ion. The present work is yet another example that shows, the utility of single-wavelength anomalous scattering data for solving a, protein structure.

About this Structure

1VKQ is a Single protein structure of sequence from Bos taurus with CA, CL and MPD as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

Reference

A redetermination of the structure of the triple mutant (K53,56,120M) of phospholipase A2 at 1.6 A resolution using sulfur-SAS at 1.54 A wavelength., Sekar K, Rajakannan V, Velmurugan D, Yamane T, Thirumurugan R, Dauter M, Dauter Z, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1586-90. Epub 2004, Aug 26. PMID:15333929

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