ArticleActa crystallographica. Section D, Biological crystallography2013
Ultratight crystal packing of a 10 kDa protein.
Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- High-resolution structure of a Kazal-type serine protease inhibitor from the dengue vector Aedes aegypti.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural and Functional Characterization of the Hazelnut Allergen Cor a 8.Journal of agricultural and food chemistry · 2015Article
- Diversity, Structures, and Collagen-Degrading Mechanisms of Bacterial Collagenolytic Proteases.Applied and environmental microbiology · 2015Review
- Structure and mechanism of cysteine peptidase gingipain K (Kgp), a major virulence factor of Porphyromonas gingivalis in periodontitis.The Journal of biological chemistry · 2014Article
- Crystallization and preliminary X-ray crystallographic analysis of PBPD2 from Listeria monocytogenes.Acta crystallographica. Section F, Structural biology communications · 2014Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While small organic molecules generally crystallize forming tightly packed lattices with little solvent content, proteins form air-sensitive high-solvent-content crystals. Here, the crystallization and full structure analysis of a novel recombinant 10 kDa protein corresponding to the C-terminal domain of a putative U32 peptidase are reported. The orthorhombic crystal contained only 24.5% solvent and is therefore among the most tightly packed protein lattices ever reported.
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