Abstract:
:Antifreeze proteins have the ability to bind to ice with high affinity and inhibit further crystal growth. The insect antifreeze protein from spruce budworm exhibits very high thermal hysteresis activity and is implicated in the protection of overwintering larvae from freezing. This protein has been crystallized in 20-25% polyethylene glycol (Mr 6000), 0.4 M NaCl, 0.1 M Tris-HCl, pH 8.5, by vapor diffusion using the hanging drop method. The resulting crystals are very thin (typically <0.01 mm in the shortest dimension), and only after repeated seeding could crystals be grown large enough for data collection using synchrotron radiation. The crystals belong to the monoclinic space group C2, with cell dimensions a = 82.28 A, b = 62.29 A, c = 63.63 A, and beta = 113.7 degrees. Molecules in the asymmetric unit are related by a twofold axis of symmetry with two molecules present. Native data to a resolution of 2.6 A have been collected with 90.3% completeness and a Rsym of 6.9%.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Graether SP,Ye Q,Davies PL,Jia Zdoi
10.1006/jsbi.1999.4087keywords:
subject
Has Abstractpub_date
1999-06-01 00:00:00pages
72-5issue
1eissn
1047-8477issn
1095-8657pii
S1047-8477(99)94087-Xjournal_volume
126pub_type
杂志文章abstract::This article has been withdrawn at the request of the author(s) and/or editor. The Publisher apologizes for any inconvenience this may cause. The full Elsevier Policy on Article Withdrawal can be found at http://www.elsevier.com/locate/withdrawalpolicy. ...
journal_title:Journal of structural biology
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abstract::The collagen which forms the egg case of the dogfish, Scyliorhinus canicula, is assembled in a three-dimensional network that results in a very resistant capsule. The capsule presumably accomplishes both a protective and a filtering role for the embryo contained within it. In the present work we have obtained electron...
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