Application of in situ diffraction in high-throughput structure determination platforms

TY - JOUR

T1 - Application of in situ diffraction in high-throughput structure determination platforms

AU - Aller, Pierre

AU - Sanchez-Weatherby, Juan

AU - Foadi, James

AU - Winter, Graeme

AU - Lobley, Carina M C

AU - Axford, Danny

AU - Ashton, Alun W

AU - Bellini, Domenico

AU - Brandao-Neto, Jose

AU - Culurgioni, Simone

AU - Douangamath, Alice

AU - Duman, Ramona

AU - Evans, Gwyndaf

AU - Fisher, Stuart

AU - Flaig, Ralf

AU - Hall, David R

AU - Lukacik, Petra

AU - Mazzorana, Marco

AU - McAuley, Katherine E

AU - Mykhaylyk, Vitaliy

AU - Owen, Robin L

AU - Paterson, Neil G

AU - Romano, Pierpaolo

AU - Sandy, James

AU - Sorensen, Thomas

AU - von Delft, Frank

AU - Wagner, Armin

AU - Warren, Anna

AU - Williams, Mark

AU - Stuart, David I

AU - Walsh, Martin A

PY - 2015

Y1 - 2015

N2 - Macromolecular crystallography (MX) is the most powerful technique available to structural biologists to visualize in atomic detail the macromolecular machinery of the cell. Since the emergence of structural genomics initiatives, significant advances have been made in all key steps of the structure determination process. In particular, third-generation synchrotron sources and the application of highly automated approaches to data acquisition and analysis at these facilities have been the major factors in the rate of increase of macromolecular structures determined annually. A plethora of tools are now available to users of synchrotron beamlines to enable rapid and efficient evaluation of samples, collection of the best data, and in favorable cases structure solution in near real time. Here, we provide a short overview of the emerging use of collecting X-ray diffraction data directly from the crystallization experiment. These in situ experiments are now routinely available to users at a number of synchrotron MX beamlines. A practical guide to the use of the method on the MX suite of beamlines at Diamond Light Source is given.

AB - Macromolecular crystallography (MX) is the most powerful technique available to structural biologists to visualize in atomic detail the macromolecular machinery of the cell. Since the emergence of structural genomics initiatives, significant advances have been made in all key steps of the structure determination process. In particular, third-generation synchrotron sources and the application of highly automated approaches to data acquisition and analysis at these facilities have been the major factors in the rate of increase of macromolecular structures determined annually. A plethora of tools are now available to users of synchrotron beamlines to enable rapid and efficient evaluation of samples, collection of the best data, and in favorable cases structure solution in near real time. Here, we provide a short overview of the emerging use of collecting X-ray diffraction data directly from the crystallization experiment. These in situ experiments are now routinely available to users at a number of synchrotron MX beamlines. A practical guide to the use of the method on the MX suite of beamlines at Diamond Light Source is given.

KW - Automation, Laboratory

KW - Crystallography, X-Ray/instrumentation

KW - Macromolecular Substances/chemistry

KW - Proteomics/instrumentation

KW - Software

KW - Synchrotrons/instrumentation

U2 - 10.1007/978-1-4939-2230-7_13

DO - 10.1007/978-1-4939-2230-7_13

M3 - Review

C2 - 25502203

SN - 1064-3745

VL - 1261

SP - 233

EP - 253

JO - Methods in molecular biology (Clifton, N.J.)

JF - Methods in molecular biology (Clifton, N.J.)

ER -