✦ LIBER ✦

Strategy for membrane protein crystallization exemplified with OmpA and OmpX

✍ Scribed by Alex Pautsch; Joachim Vogt; Kirstin Model; Christian Siebold; Georg E. Schulz

Publisher: John Wiley and Sons
Year: 1999
Tongue: English
Weight: 239 KB
Volume: 34
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(19990201)34:2<167::aid-prot2>3.0.co;2-h

No coin nor oath required. For personal study only.

✦ Synopsis

The bacterial outer membrane proteins OmpA and OmpX were modified in such a manner that they yielded bulky crystals diffracting X-rays isotropically beyond 2 A resolution and permitting detailed structural analyses. The procedure involved semi-directed mutagenesis, mass production into inclusion bodies, and (re)naturation therefrom; it should be applicable for a broader range of membrane proteins.

📜 SIMILAR VOLUMES

Site-directed 13C solid-state NMR studie

Site-directed 13C solid-state NMR studies on membrane proteins: strategy and goals toward revealing conformation and dynamics as illustrated for bacteriorhodopsin labeled with [1-13C]amino acid residues

✍ Hazime Saitô; Jun Mikami; Satoru Yamaguchi; Michikazu Tanio; Atushi Kira; Tadash 📂 Article 📅 2004 🏛 John Wiley and Sons 🌐 English ⚖ 419 KB

## Abstract We have so far demonstrated that well‐resolved and site‐specifically assigned ^13^C peaks as recorded by site‐directed NMR study on ^13^C‐labeled membrane proteins can serve as a convenient probe to reveal their local conformation and dynamics. We attempted here to clarify the extent to