Mutant/mutation
This mutant lacks expression of both p230 and p230p and expresses GFP-luciferase under the control of the constitutive eef1a promoter.
The p230 gene is disrupted in parasites of the the 676m1cl1 (RMgm-29) that contains a  GFP-luciferase expression cassette integrated into the p230p gene. This  line does not contain a drug-selectable marker. The p230 gene is disrupted using a construct that was used to generate mutant RMgm-350.

Phenotype
In rodent malaria parasites both P230 and P230p are expressed in male gametocytes/gametes.
The single p230p KO mutant produces fertile gametes, that attach to red blood cells (forming exflagellation centers) and shows a phenotype throughout the complete life cycle that is not different from that of wild type parasites (see also PMID 20386715).
The single p230 KO mutant produces gametes that are NOT fertile. They attach to red blood cells (forming exflagellation centers) but fail to recognise/attach to female gametes (see also PMID 20386715 and RMgm-350).

The double KO mutant PbΔp230Δp230p produces normal numbers of gametocytes and male gametocytes form male gamete numbers (by the process of exflagelllation) comparable to that of wild type parasites. In addition, male gametes attach to red blood cells (forming exflagellation centers) but fail to recognise/attach to female gametes.

Additional information
From the paper:
'The role of P230 and P230p in P. falciparum gamete binding to RBC is different to the role of these proteins in the rodent parasite P. berghei (see PMID 30297725) . Single gene-deletion mutants lacking expression of either P230 or P230p in P. berghei exhibit formation of exflagellation centres like WT, indicating that male gametes of these mutants bind normally to RBC. To examine a possible compensatory role in RBC binding of the two P. berghei paralogs we generated a p230 and p230p double gene deletion mutant. Activated male gametocytes of this mutant, PbΔp230Δp230p, formed WT-like levels of exflagellation centres demonstrating an absence of a role of these proteins in RBC binding of P. berghei male gametes'.