Comparison of the dynamics of myoglobin in different crystal forms.
Crystals have been grown of "sperm whale" myoglobin produced in Escherichia coli from a synthetic gene and the structure has been solved to 1.9 A resolution. Because of a remaining initiator methionine, this protein crystallizes in a different space group from native sperm whale myoglobin....
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ftpubmed:oai:pubmedcentral.nih.gov:1280679 2023-05-15T18:26:32+02:00 Comparison of the dynamics of myoglobin in different crystal forms. Phillips, G N 1990-02 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1280679 http://www.ncbi.nlm.nih.gov/pubmed/2180490 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1280679 http://www.ncbi.nlm.nih.gov/pubmed/2180490 Research Article Text 1990 ftpubmed 2013-08-30T16:57:19Z Crystals have been grown of "sperm whale" myoglobin produced in Escherichia coli from a synthetic gene and the structure has been solved to 1.9 A resolution. Because of a remaining initiator methionine, this protein crystallizes in a different space group from native sperm whale myoglobin. The three-dimensional structure of the synthetic protein is essentially identical to the native sperm whale protein. However, the crystallographic B-factors for parts of the molecule are quite different in the two crystal forms, and provide a measure of the effect of different packing constraints on the flexibility of the protein. The effect of the packing forces is to reduce the mobility of the protein in the regions of contact and thereby introduce differences in mobilities between the two crystal forms. Discrepancies between mobilities calculated from molecular dynamics simulations and crystallography can be reduced by considering the data from both crystal forms. Text Sperm whale PubMed Central (PMC) |
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Research Article |
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Research Article Phillips, G N Comparison of the dynamics of myoglobin in different crystal forms. |
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Research Article |
description |
Crystals have been grown of "sperm whale" myoglobin produced in Escherichia coli from a synthetic gene and the structure has been solved to 1.9 A resolution. Because of a remaining initiator methionine, this protein crystallizes in a different space group from native sperm whale myoglobin. The three-dimensional structure of the synthetic protein is essentially identical to the native sperm whale protein. However, the crystallographic B-factors for parts of the molecule are quite different in the two crystal forms, and provide a measure of the effect of different packing constraints on the flexibility of the protein. The effect of the packing forces is to reduce the mobility of the protein in the regions of contact and thereby introduce differences in mobilities between the two crystal forms. Discrepancies between mobilities calculated from molecular dynamics simulations and crystallography can be reduced by considering the data from both crystal forms. |
format |
Text |
author |
Phillips, G N |
author_facet |
Phillips, G N |
author_sort |
Phillips, G N |
title |
Comparison of the dynamics of myoglobin in different crystal forms. |
title_short |
Comparison of the dynamics of myoglobin in different crystal forms. |
title_full |
Comparison of the dynamics of myoglobin in different crystal forms. |
title_fullStr |
Comparison of the dynamics of myoglobin in different crystal forms. |
title_full_unstemmed |
Comparison of the dynamics of myoglobin in different crystal forms. |
title_sort |
comparison of the dynamics of myoglobin in different crystal forms. |
publishDate |
1990 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1280679 http://www.ncbi.nlm.nih.gov/pubmed/2180490 |
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Sperm whale |
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Sperm whale |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1280679 http://www.ncbi.nlm.nih.gov/pubmed/2180490 |
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1766208502656663552 |