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Title: Identifying, studying and making good use of macromolecular crystals

As technology advances, the crystal volume that can be used to collect useful X-ray diffraction data decreases. The technologies available to detect and study growing crystals beyond the optical resolution limit and methods to successfully place the crystal into the X-ray beam are discussed. Structural biology has contributed tremendous knowledge to the understanding of life on the molecular scale. The Protein Data Bank, a depository of this structural knowledge, currently contains over 100 000 protein structures, with the majority stemming from X-ray crystallography. As the name might suggest, crystallography requires crystals. As detectors become more sensitive and X-ray sources more intense, the notion of a crystal is gradually changing from one large enough to embellish expensive jewellery to objects that have external dimensions of the order of the wavelength of visible light. Identifying these crystals is a prerequisite to their study. This paper discusses developments in identifying these crystals during crystallization screening and distinguishing them from other potential outcomes. The practical aspects of ensuring that once a crystal is identified it can then be positioned in the X-ray beam for data collection are also addressed.
Authors:
 [1] ;  [2] ;  [3] ;  [4] ;  [5] ;  [3] ;  [4] ;  [4]
  1. University of Pittsburgh Medical School, Pittsburgh, PA 15261 (United States)
  2. SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025 (United States)
  3. Hauptman–Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, NY 14203 (United States)
  4. (United States)
  5. CSIRO Collaborative Crystallisation Centre, 343 Royal Parade, Parkville, Victoria 3052 (Australia)
Publication Date:
OSTI Identifier:
22375694
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta crystallographica. Section F, Structural biology communications; Journal Volume: 70; Journal Issue: Pt 8; Other Information: PMCID: PMC4118793; PMID: 25084371; PUBLISHER-ID: en5553; OAI: oai:pubmedcentral.nih.gov:4118793; Copyright (c) Calero et al. 2014; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; BEAMS; CRYSTAL GROWTH; CRYSTALLIZATION; CRYSTALLOGRAPHY; CRYSTALS; POTENTIALS; PROTEIN STRUCTURE; PROTEINS; RESOLUTION; SCREENING; VISIBLE RADIATION; WAVELENGTHS; X-RAY DIFFRACTION; X-RAY SOURCES