High resolution imaging as a characterization tool for biological crystals.
Biomolecular crystals consist of large unit cells that form a rather flexible medium that is able to accommodate a certain degree of lattice distortion, leading to several interesting issues ranging from structural to physical properties. Several techniques, from X-ray diffraction to microscopy, have been adapted to study the structural and physical properties of biomolecular crystals systematically. The use of synchrotron-based monochromatic X-ray diffraction topography, with triple axis diffractometry and rocking curve measurements, to characterize biomolecular crystals is reviewed. Recent X-ray diffraction images from gel and solution grown lysozyme crystals are presented. Defect structures in these crystals are discussed, together with reciprocal space mapping, and compared with results obtained from crystals grown in a low gravity environment.
Stojanoff
Vivian
V
National Synchrotron Light Source, Brookhaven National Laboratories, Upton, NY 11973, USA. stojanof@bnl.gov
Cappelle
B
B
Epelboin
Y
Y
Hartwig
J
J
Moradela
A B
AB
Otalora
F
F
D000818:Animals; D001703:Biophysics / Q000379:methods*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004529:Egg White; D007091:Image Processing, Computer-Assisted / Q000379:methods*; D018625:Microscopy, Atomic Force; D009113:Muramidase / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012825:Silicon / Q000737:chemistry; D014422:Turkeys; D014893:Weightlessness; D014961:X-Ray Diffraction / Q000379:methods; D014965:X-Rays
D011506:Proteins; D009113:Muramidase; D012825:Silicon