The X-ray crystal structures of perdeuteriated and protiated enzyme elongation factor Tu are very similar

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Abstract

X-Ray structural comparisons show that perdeuteriation does not affect the overall fold or domain arrangement of elongation factor Tu.

@article{07d8b20fd68c45c8ae2a159d29d94209,

title = "The X-ray crystal structures of perdeuteriated and protiated enzyme elongation factor Tu are very similar",

abstract = "X-Ray structural comparisons show that perdeuteriation does not affect the overall fold or domain arrangement of elongation factor Tu.",

author = "Cooper, \{Serena J.\} and David Brockwell and James Raftery and David Attwood and Jill Barber and Helliwell, \{John R.\}",

year = "1998",

month = may,

day = "21",

language = "English",

pages = "1063--1064",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "10",

}

TY - JOUR

T1 - The X-ray crystal structures of perdeuteriated and protiated enzyme elongation factor Tu are very similar

AU - Cooper, Serena J.

AU - Brockwell, David

AU - Raftery, James

AU - Attwood, David

AU - Barber, Jill

AU - Helliwell, John R.

PY - 1998/5/21

Y1 - 1998/5/21

N2 - X-Ray structural comparisons show that perdeuteriation does not affect the overall fold or domain arrangement of elongation factor Tu.

AB - X-Ray structural comparisons show that perdeuteriation does not affect the overall fold or domain arrangement of elongation factor Tu.

M3 - Article

SN - 1359-7345

SP - 1063

EP - 1064

JO - Chemical Communications

JF - Chemical Communications

IS - 10

ER -