ABSTRACT
BACKGROUND: Environmental contamination of patient rooms and adjacent areas with C. difficile spores is a recognized transmission risk. Previous studies have shown that spores are aerosolized during patient care. These spores can remain airborne for extended periods and may contaminate distant surfaces. High-volume air sampling equipment allows for the collection of a large volume of air and was evaluated in the collection of C. difficile aerosol. METHOD: Air samplers evaluated in this research included the DFU-1000, XMX/2L-MIL, Biocapture-650, and a MB2. Aerosols of C. difficile were generated in a 5-m3 chamber and each air sampler sampled in the aerosol test chamber simultaneously with referee air samplers. RESULTS: The DFU-1000 achieved the highest efficiency of the 4 air samplers (Pâ¯=â¯.0145) with a mean efficiency of 38.60%. The relative efficiencies of the Biocapture-650, XMX/2L-MIL, and MB2 were 28.16%, 10.51%, and 3.05%, respectively. DISCUSSION/CONCLUSIONS: This study demonstrated high variation based on the sampling method employed. Based on the results of these studies, high-volume air samplers may be effectively applied to sample for airborne C. difficile in health care environments. The high sampling flow rate of the DFU-1000 would allow for the complete sampling of a patient room-sized volume in less than 1 hour.
Subject(s)
Clostridioides difficile , Clostridioides , Aerosols/analysis , Delivery of Health Care , Environmental Monitoring , Humans , Spores, BacterialABSTRACT
The NewProt protein engineering portal is a one-stop-shop for in silico protein engineering. It gives access to a large number of servers that compute a wide variety of protein structure characteristics supporting work on the modification of proteins through the introduction of (multiple) point mutations. The results can be inspected through multiple visualizers. The HOPE software is included to indicate mutations with possible undesired side effects. The Hotspot Wizard software is embedded for the design of mutations that modify a proteins' activity, specificity, or stability. The NewProt portal is freely accessible at http://newprot.cmbi.umcn.nl/ and http://newprot.fluidops.net/.
Subject(s)
Databases, Protein , Internet , Protein Engineering/methods , Proteins , Software , Models, Molecular , Proteins/chemistry , Proteins/genetics , Proteins/metabolism , User-Computer InterfaceABSTRACT
We present a series of databanks (http://swift.cmbi.ru.nl/gv/facilities/) that hold information that is computationally derived from Protein Data Bank (PDB) entries and that might augment macromolecular structure studies. These derived databanks run parallel to the PDB, i.e. they have one entry per PDB entry. Several of the well-established databanks such as HSSP, PDBREPORT and PDB_REDO have been updated and/or improved. The software that creates the DSSP databank, for example, has been rewritten to better cope with π-helices. A large number of databanks have been added to aid computational structural biology; some examples are lists of residues that make crystal contacts, lists of contacting residues using a series of contact definitions or lists of residue accessibilities. PDB files are not the optimal presentation of the underlying data for many studies. We therefore made a series of databanks that hold PDB files in an easier to use or more consistent representation. The BDB databank holds X-ray PDB files with consistently represented B-factors. We also added several visualization tools to aid the users of our databanks.
