skip to main content

Title: Ultratight crystal packing of a 10 kDa protein

The crystal structure of the C-terminal domain of a putative U32 peptidase from G. thermoleovorans is reported; it is one of the most tightly packed protein structures reported to date. 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.
Authors:
 [1] ;  [2] ;  [3] ;  [4] ;  [3] ;  [2] ; ; ;  [1]
  1. Molecular Biology Institute of Barcelona, Spanish Research Council CSIC, Barcelona Science Park, c/Baldiri Reixac 15-21, 08028 Barcelona (Spain)
  2. Vilnius University, M. K. Čiurlionio 21/27, 03101 Vilnius (Lithuania)
  3. University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA 22908-0736 (United States)
  4. University of South Carolina, 631 Sumter Street, Columbia, SC 29208 (United States)
Publication Date:
OSTI Identifier:
22351322
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section D: Biological Crystallography; Journal Volume: 69; Journal Issue: Pt 3; Other Information: PMCID: PMC4048058; PMID: 23519421; PUBLISHER-ID: dz5271; OAI: oai:pubmedcentral.nih.gov:4048058; Copyright (c) International Union of Crystallography 2013; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
Denmark
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; AIR; CRYSTAL STRUCTURE; CRYSTALLIZATION; CRYSTALS; MOLECULES; PROTEIN STRUCTURE; PROTEINS; SOLVENTS; STOWING