X-rays are electromagnetic radiation with wavelengths

between about 0.02 Å and 100 Å (1Å = 10-10 meters).

X-ray tube. consists of an
evacuated chamber with a tungsten
filament at one end of the tube,
called the cathode, and a metal
target at the other end, called an
anode. Electrical current is run
through the tungsten filament,
causing it to glow and emit
electrons. A large voltage difference
(measured in kilovolts) is placed
between the cathode and the anode,
causing the electrons to move at
high velocity from the filament to the
anode target. Upon striking the
atoms in the target, the electrons
dislodge inner shell electrons
resulting in outer shell electrons
having to jump to a lower energy
shell to replace the dislodged
electrons. These electronic
transitions results in the generation
of X-rays.
optical spectrum for hydrogen. The distinct lines near 435 nm, 487
nm, and 655 nm show transitions from the 5th, 4th and 3rd energy
shells, respectively, into the 2nd energy shell.
Even the most energetic line hydrogen emits (when an electron drops
down from the second shell to the first) has only enough energy to be
an ultraviolet photon.
Cartoon of a hypothetical crystalline
lattice
 Crystallisation

Diagram of hanging drop method. Reservoir solution (blue) usually contains

buffer and precipitant. Protein solution (red) contains the same compounds, but
in lower concentrations. The protein solution may also contain trace metals or
ions necessary for precipitation of particular proteins. For instance, insulin is
known to require trace amounts of zinc for crystallization (McRee, 1993).
Diagram of sitting drop method. In this method, the protein
drop sits on a pedestal above the reservoir solution, as
opposed to hanging.
 Panel 1 Region of exceptional experimental electron density map created from multi-wavelength data collected at the ALS.
Only solvent flattening and density modification have been performed. No phase combination with any model phases has
taken place. Panel 2 : .to show the excellent correspondence with actual protein residues, a previously determined
molecular replacement model of Arg has been placed into the electron density. The model can be unambiguously and easily
built into the electron density.

Panel 3 : View is a cross section of the apoE four helix bundle. The empty space in the centre of helix one and two is clearly
visible. Panel 4: : to show the excellent correspondence of experimental electron density with actual protein residues, model
helices have been placed into the electron density. Experimental phases had an average figure of merit of 0.86. There is very
little noise and excellent connectivity in the electron density.
Panel 1 : experimental electron density map created from multi-wavelength data collected
Only solvent flattening and density modification have been performed. No phase combination
with any model phases has taken place. Panel 2 : tyrosine residue fitted into experimental
electron density. Panel 3 electron density of combined MAD/MIR map in tetanus C fragment.