Fragment Collapsing and Splitting While Assembling High-Resolution Restriction Maps
- 1 January 1995
- journal article
- Published by Mary Ann Liebert Inc in Journal of Computational Biology
- Vol. 2 (2), 185-205
- https://doi.org/10.1089/cmb.1995.2.185
Abstract
In the process of constructing high-resolution restriction maps via greedy algorithms, a classical anomaly, known as fragment collapsing, introduces errors into the maps that impedes further map assembly. Fragment collapsing occurs when two different genomic fragments of approximately the same length and occurring in the digestion of two different overlapping clones are incorrectly identified as representative of a single genomic fragment. This introduces a single fragment of commensurate length into an incorrect position in the map. The present work describes techniques for detecting and correcting such anomalies.Keywords
This publication has 11 references indexed in Scilit:
- REBASE–restriction enzymes and methylasesNucleic Acids Research, 1993
- Evaluation of a cosmid contig physical map of human chromosome 16Genomics, 1992
- Spatial normalization of one-dimensional electrophoretic gel imagesGenomics, 1990
- Physical mapping of human chromosomes by repetitive sequence fingerprinting.Proceedings of the National Academy of Sciences of the United States of America, 1990
- A high-resolution, fluorescence-based, semiautomated method for DNA fingerprintingGenomics, 1989
- The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic libraryCell, 1987
- Random-clone strategy for genomic restriction mapping in yeast.Proceedings of the National Academy of Sciences of the United States of America, 1986
- Toward a physical map of the genome of the nematode Caenorhabditis elegansProceedings of the National Academy of Sciences of the United States of America, 1986
- A restriction enzyme from Hemophilus influenzae: II. Base sequence of the recognition siteJournal of Molecular Biology, 1970
- A Restriction enzyme from Hemophilus influenzae: I. Purification and general propertiesJournal of Molecular Biology, 1970