Room Temperature X-Ray Crystallography Reveals Conformational Heterogeneity of Engineered Proteins

Thomas Szyperski

doi:10.1016/j.str.2017.04.004

Room Temperature X-Ray Crystallography Reveals Conformational Heterogeneity of Engineered Proteins

Thomas Szyperski

Chemistry

Research output: Contribution to journal › Short survey › peer-review

2 Scopus citations

Abstract

In this issue of Structure, Biel et al. (2017) present multi-conformer analyses from room temperature X-ray data of two ubiquitin phage display variants binding deubiquitinase USP7. The first contains core mutations. The second matured variant contains additional surface mutations. Alternate conformations detected in the core mutant were removed by maturation.

Original language	English
Pages (from-to)	691-692
Number of pages	2
Journal	Structure
Volume	25
Issue number	5
DOIs	https://doi.org/10.1016/j.str.2017.04.004
State	Published - May 2 2017

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title = "Room Temperature X-Ray Crystallography Reveals Conformational Heterogeneity of Engineered Proteins",

abstract = "In this issue of Structure, Biel et al. (2017) present multi-conformer analyses from room temperature X-ray data of two ubiquitin phage display variants binding deubiquitinase USP7. The first contains core mutations. The second matured variant contains additional surface mutations. Alternate conformations detected in the core mutant were removed by maturation.",

author = "Thomas Szyperski",

note = "Publisher Copyright: {\textcopyright} 2017 Elsevier Ltd",

year = "2017",

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AU - Szyperski, Thomas

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N2 - In this issue of Structure, Biel et al. (2017) present multi-conformer analyses from room temperature X-ray data of two ubiquitin phage display variants binding deubiquitinase USP7. The first contains core mutations. The second matured variant contains additional surface mutations. Alternate conformations detected in the core mutant were removed by maturation.

AB - In this issue of Structure, Biel et al. (2017) present multi-conformer analyses from room temperature X-ray data of two ubiquitin phage display variants binding deubiquitinase USP7. The first contains core mutations. The second matured variant contains additional surface mutations. Alternate conformations detected in the core mutant were removed by maturation.

UR - https://www.scopus.com/pages/publications/85018431145

U2 - 10.1016/j.str.2017.04.004

DO - 10.1016/j.str.2017.04.004

M3 - Short survey

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AN - SCOPUS:85018431145

SN - 0969-2126

VL - 25

SP - 691

EP - 692

JO - Structure

JF - Structure

IS - 5

ER -

Room Temperature X-Ray Crystallography Reveals Conformational Heterogeneity of Engineered Proteins

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