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.
Original language | English |
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Pages (from-to) | 464-470 |
Number of pages | 7 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 69 |
Issue number | 3 |
DOIs | |
State | Published - Mar 2013 |
Externally published | Yes |
Keywords
- crystal packing
- high resolution
- solvent content