Crystallization and preliminary X-ray diffraction studies of a toxic phospholipase A2 from the venom of Vipera ammodytes meridionalis complexed to a synthetic inhibitor
β Scribed by Dessislava Nikolova Georgieva; Wojciech Rypniewski; Markus Perbandt; Mahendra Jain; Nicolay Genov; Christian Betzel
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 86 KB
- Volume
- 1650
- Category
- Article
- ISSN
- 1570-9639
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β¦ Synopsis
A toxic phospholipase A(2) (PLA(2)) is isolated from the neurotoxic complex Vipoxin, the major lethal component of the venom of Vipera ammodytes meridionalis. The enzyme is complexed to the synthetic inhibitor elaidoylamide and crystallized. The crystals belong to the space group P2(1)2(1)2(1), with unit cell dimensions a=46.57 A, b=82.68 A, c=119.47 A and beta=90 degrees. Initial diffraction data to 3.3 A resolution are collected.
π SIMILAR VOLUMES
An acidic phospholipase A 2 (PLA 2 ) isolated from Bothrops jararacussu snake venom was crystallized with two inhibitors: a-tocopherol (vitamin E) and p-bromophenacyl bromide (BPB). The crystals diffracted at 1.45-and 1.85-A Λresolution, respectively, for the complexes with a-tocopherol and p-bromop