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Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography	New Insights into the Structure of the Reaction Centre from Blastochloris viridis: Evolution in the Laboratory Aleksander Roszak , Vladimira Moulisova , Adhie Reksodipuro , Alastair Gardiner , Ritsuko Fujii , Hideki Hashimoto , Neil W. Isaacs , Richard J. Cogdell Biochemical Journal DOI: 10.1042/BJ20111540 PMID: 22054235 Diamond Proposal Number(s): [1229] Show Abstract ▼ Abstract: Newly determined crystal structures of the photosynthetic RC (reaction centre) from two substrains of the non-sulfur purple bacterium Blastochloris viridis strain DSM 133, together with analysis of their gene sequences, has revealed intraspecies evolutionary changes over a period of 14 years. Over 100 point mutations were identified between these two substrains in the four genes encoding the protein subunits of the RC, of which approximately one-fifth resulted in a total of 16 amino acid changes. The most interesting difference was in the M subunit where the change from a leucine residue to glycine in the carotenoid-binding pocket allowed NS5 (1,2-dihydroneurosporene) to adopt a more sterically favoured conformation, similar to the carotenoid conformation found in other related RCs. The results of the present study, together with a high rate of mutations in laboratory bacterial cultures described recently, suggest that bacteria evolve faster than has been generally recognized. The possibility that amino acid changes occur within protein sequences, without exhibiting any immediately observable phenotype, should be taken into account in studies that involve long-term continuous growth of pure bacterial cultures. The Blc. viridis RC is often studied with sophisticated biophysical techniques and changes such as those described here may well affect their outcome. In other words, there is a danger that laboratory-to-laboratory variation could well be due to different groups not realising that they are actually working with slightly different proteins. A way around this problem is suggested.	Nov 2011
I03-Macromolecular Crystallography	High-throughput identification of purification conditions leads to preliminary crystallization conditions for three inner membrane proteins Mads Gabrielsen , Frank Kroner , Isobel Black , Neil Isaacs , Andrew J. Roe , Karen McLuskey Molecular Membrane Biology 28 (7-8), 445 - 453 DOI: 10.3109/09687688.2011.628954 PMID: 22034843 Show Abstract ▼ Abstract: An important factor in the crystallization, and subsequent structural determination, of integral membrane proteins is the ability to produce a stable and monodisperse solution of the protein. Obtaining the correct purification detergent to achieve this can be laborious and is often serendipitous. In this study, high-throughput methods are used to analyze the suitability of eight different detergents on the stability of 12 inner transmembrane proteins from Escherichia coli. The best results obtained from the small-scale experiments were scaled up, the aggregation state of the proteins assessed, and all monodisperse protein solutions entered into crystallization trials. This resulted in preliminary crystallization hits for three inner membrane proteins: XylH, PgpB and YjdL and this study reports the methods, purification procedures and crystallization conditions used to achieve this.	Oct 2011

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