Crystallization and preliminary X-ray diffraction study of an active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon
- 18 August 2006
- journal article
- crystallization communications
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 62 (9) , 902-905
- https://doi.org/10.1107/s1744309106030454
Abstract
Crystallization of and preliminary crystallographic studies on an active-site mutant of pro-Tk-subtilisin from the hyperthermophilic archaeon Thermococcus kodakaraensis were performed. The crystal was grown at 277 K by the sitting-drop vapour-diffusion method. Native X-ray diffraction data were collected to 2.3 Å resolution using synchrotron radiation from station BL41XU at SPring-8. The crystal belongs to the orthorhombic space group I222, with unit-cell parameters a = 92.69, b = 121.78, c = 77.53 Å. Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient V M was calculated to be 2.6 Å3 Da-1 and the solvent content was 53.1%.Keywords
This publication has 28 references indexed in Scilit:
- Functional Analysis of the Propeptide of Subtilisin E as an Intramolecular Chaperone for Protein FoldingPublished by Elsevier ,1995
- Folding Pathway Mediated by an Intramolecular Chaperone: Characterization of the Structural Changes in Pro-subtilisin E Coincident with Autoprocess ingJournal of Molecular Biology, 1995
- Folding of Subtilisin BPN': Role of the Pro-sequenceJournal of Molecular Biology, 1993
- Calcium‐independent subtilisin by designProteins-Structure Function and Bioinformatics, 1993
- GENE-SPLICING BY OVERLAP EXTENSION - TAILOR-MADE GENES USING THE POLYMERASE CHAIN-REACTION1990
- Activity and Deletion Analysis of Recombinant Human Cathepsin L Expressed in Escherichia coliJournal of Biological Chemistry, 1989
- Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 Å resolution and comparison of two crystal forms that differ in calcium contentJournal of Molecular Biology, 1989
- The αlytic protease pro-region does not require a physical linkage to activate the protease domain in vivoNature, 1989
- The high‐resolution X‐ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalisEuropean Journal of Biochemistry, 1987
- Role of bound calcium ions in thermostable, proteolytic enzymes. Separation of intrinsic and calcium ion contributions to the kinetic thermal stabilityBiochemistry, 1976