Comparison of the dynamics of myoglobin in different crystal forms.

Abstract:

: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.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Phillips GN Jr

doi

10.1016/S0006-3495(90)82540-6

subject

Has Abstract

pub_date

1990-02-01 00:00:00

pages

381-3

issue

2

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(90)82540-6

journal_volume

57

pub_type

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